메뉴 건너뛰기




Volumn 1813, Issue 10, 2011, Pages 1893-1905

Urban planning of the endoplasmic reticulum (ER): How diverse mechanisms segregate the many functions of the ER

Author keywords

Endoplasmic reticulum (ER); Lipid droplet; Mitochondria associated membrane (MAM); Plasma membrane associated membrane (PAM); Russell bodies

Indexed keywords

ATLASTIN; BIOLOGICAL MARKER; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; CALNEXIN; FAT DROPLET; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; MEMBRANE PROTEIN; MITOFUSIN 2; NESPRIN; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 2; PRESENILIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN IRE1; RAB32 PROTEIN; RIBOPHORIN I; RIBOPHORIN II; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; STROMAL INTERACTION MOLECULE 1; UNCLASSIFIED DRUG; VALOSIN CONTAINING PROTEIN;

EID: 80051788173     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.06.011     Document Type: Review
Times cited : (111)

References (266)
  • 1
    • 0027078786 scopus 로고
    • Endoplasmic reticulum: a dynamic patchwork of specialized subregions
    • Sitia R., Meldolesi J. Endoplasmic reticulum: a dynamic patchwork of specialized subregions. Mol. Biol. Cell. 1992, 3:1067-1072.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1067-1072
    • Sitia, R.1    Meldolesi, J.2
  • 2
    • 34047152917 scopus 로고
    • Structure and connections of neurons
    • Ramon Y.C.S. Structure and connections of neurons. Bull. Los Angel. Neuro. Soc. 1952, 17:5-46.
    • (1952) Bull. Los Angel. Neuro. Soc. , vol.17 , pp. 5-46
    • Ramon, Y.C.S.1
  • 3
    • 85025399883 scopus 로고
    • A study of tissue culture cells by electron microscopy: methods and preliminary observations
    • Porter K.R., Claude A., Fullam E.F. A study of tissue culture cells by electron microscopy: methods and preliminary observations. J. Exp. Med. 1945, 81:233-246.
    • (1945) J. Exp. Med. , vol.81 , pp. 233-246
    • Porter, K.R.1    Claude, A.2    Fullam, E.F.3
  • 4
    • 29344439641 scopus 로고
    • Significance of cell particulates as seen by electron microscopy
    • Porter K.R., Kallman F.L. Significance of cell particulates as seen by electron microscopy. Ann. N. Y. Acad. Sci. 1952, 54:882-891.
    • (1952) Ann. N. Y. Acad. Sci. , vol.54 , pp. 882-891
    • Porter, K.R.1    Kallman, F.L.2
  • 5
    • 75449124557 scopus 로고
    • Isolation and properties of rough and smooth vesicles from rat liver
    • Dallner G., Orrenius S., Bergstrand A. Isolation and properties of rough and smooth vesicles from rat liver. J. Cell Biol. 1963, 16:426-430.
    • (1963) J. Cell Biol. , vol.16 , pp. 426-430
    • Dallner, G.1    Orrenius, S.2    Bergstrand, A.3
  • 6
    • 0000628018 scopus 로고
    • Liver microsomes; an integrated morphological and biochemical study
    • Palade G.E., Siekevitz P. Liver microsomes; an integrated morphological and biochemical study. J. Biophys. Biochem. Cytol. 1956, 2:171-200.
    • (1956) J. Biophys. Biochem. Cytol. , vol.2 , pp. 171-200
    • Palade, G.E.1    Siekevitz, P.2
  • 7
    • 12644292519 scopus 로고
    • The constitution of protoplasm
    • Claude A. The constitution of protoplasm. Science 1943, 97:451-456.
    • (1943) Science , vol.97 , pp. 451-456
    • Claude, A.1
  • 8
    • 3242807744 scopus 로고
    • The nuclear envelope; its structure and relation to cytoplasmic membranes
    • Watson M.L. The nuclear envelope; its structure and relation to cytoplasmic membranes. J. Biophys. Biochem. Cytol. 1955, 1:257-270.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 257-270
    • Watson, M.L.1
  • 9
    • 64749091534 scopus 로고    scopus 로고
    • ER membrane-bending proteins are necessary for de novo nuclear pore formation
    • Dawson T.R., Lazarus M.D., Hetzer M.W., Wente S.R. ER membrane-bending proteins are necessary for de novo nuclear pore formation. J. Cell Biol. 2009, 184:659-675.
    • (2009) J. Cell Biol. , vol.184 , pp. 659-675
    • Dawson, T.R.1    Lazarus, M.D.2    Hetzer, M.W.3    Wente, S.R.4
  • 10
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel G., Dobberstein B. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 1975, 67:852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 11
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 1975, 67:835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 12
    • 0014384434 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis
    • Jamieson J.D., Palade G.E. Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis. J. Cell. Biol. 1968, 39:580-588.
    • (1968) J. Cell. Biol. , vol.39 , pp. 580-588
    • Jamieson, J.D.1    Palade, G.E.2
  • 13
    • 0022827170 scopus 로고
    • Mechanism of protein translocation across the endoplasmic reticulum membrane
    • Walter P., Lingappa V.R. Mechanism of protein translocation across the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 1986, 2:499-516.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 499-516
    • Walter, P.1    Lingappa, V.R.2
  • 14
    • 0017691189 scopus 로고
    • Localization of the enzyme system for glycosylation of proteins via the lipid-linked pathway in rough endoplasmic reticulum
    • Czichi U., Lennarz W.J. Localization of the enzyme system for glycosylation of proteins via the lipid-linked pathway in rough endoplasmic reticulum. J. Biol. Chem. 1977, 252:7901-7904.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7901-7904
    • Czichi, U.1    Lennarz, W.J.2
  • 15
    • 33746778834 scopus 로고    scopus 로고
    • Rough sheets and smooth tubules
    • Shibata Y., Voeltz G.K., Rapoport T.A. Rough sheets and smooth tubules. Cell 2006, 126:435-439.
    • (2006) Cell , vol.126 , pp. 435-439
    • Shibata, Y.1    Voeltz, G.K.2    Rapoport, T.A.3
  • 17
    • 71649112895 scopus 로고    scopus 로고
    • 3D tomography reveals connections between the phagophore and endoplasmic reticulum
    • Yla-Anttila P., Vihinen H., Jokitalo E., Eskelinen E.L. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 2009, 5:1180-1185.
    • (2009) Autophagy , vol.5 , pp. 1180-1185
    • Yla-Anttila, P.1    Vihinen, H.2    Jokitalo, E.3    Eskelinen, E.L.4
  • 18
    • 0013785336 scopus 로고
    • Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes, a morphological and biochemical study
    • Orrenius S., Ericsson J.L., Ernster L. Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes, a morphological and biochemical study. J. Cell Biol. 1965, 25:627-639.
    • (1965) J. Cell Biol. , vol.25 , pp. 627-639
    • Orrenius, S.1    Ericsson, J.L.2    Ernster, L.3
  • 19
    • 0343815128 scopus 로고
    • Epoxide hydrolase is a marker for the smooth endoplasmic reticulum in rat liver
    • Galteau M.M., Antoine B., Reggio H. Epoxide hydrolase is a marker for the smooth endoplasmic reticulum in rat liver. EMBO J. 1985, 4:2793-2800.
    • (1985) EMBO J. , vol.4 , pp. 2793-2800
    • Galteau, M.M.1    Antoine, B.2    Reggio, H.3
  • 20
    • 0013899589 scopus 로고
    • The ultrastructure of fatty liver induced by prolonged ethanol ingestion
    • Iseri O.A., Lieber C.S., Gottlieb L.S. The ultrastructure of fatty liver induced by prolonged ethanol ingestion. Am. J. Pathol. 1966, 48:535-555.
    • (1966) Am. J. Pathol. , vol.48 , pp. 535-555
    • Iseri, O.A.1    Lieber, C.S.2    Gottlieb, L.S.3
  • 21
    • 7544222395 scopus 로고    scopus 로고
    • The discovery of the microsomal ethanol oxidizing system and its physiologic and pathologic role
    • Lieber C.S. The discovery of the microsomal ethanol oxidizing system and its physiologic and pathologic role. Drug Metab. Rev. 2004, 36:511-529.
    • (2004) Drug Metab. Rev. , vol.36 , pp. 511-529
    • Lieber, C.S.1
  • 22
    • 0027499273 scopus 로고
    • Induction of cytochrome P-4502E1 in the human liver by ethanol is caused by a corresponding increase in encoding messenger RNA
    • Takahashi T., Lasker J.M., Rosman A.S., Lieber C.S. Induction of cytochrome P-4502E1 in the human liver by ethanol is caused by a corresponding increase in encoding messenger RNA. Hepatology 1993, 17:236-245.
    • (1993) Hepatology , vol.17 , pp. 236-245
    • Takahashi, T.1    Lasker, J.M.2    Rosman, A.S.3    Lieber, C.S.4
  • 23
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E., Romijn E.P., Maggioni C., Mezghrani A., Sitia R., Braakman I., Heck A.J. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity 2003, 18:243-253.
    • (2003) Immunity , vol.18 , pp. 243-253
    • van Anken, E.1    Romijn, E.P.2    Maggioni, C.3    Mezghrani, A.4    Sitia, R.5    Braakman, I.6    Heck, A.J.7
  • 24
    • 0016274490 scopus 로고
    • Studies on the biogenesis of smooth endoplasmic reticulum membranes in hepatocytes of phenobarbital-treated rats. II. The site of phospholipid synthesis in the initial phase of membrane proliferation
    • Higgins J.A. Studies on the biogenesis of smooth endoplasmic reticulum membranes in hepatocytes of phenobarbital-treated rats. II. The site of phospholipid synthesis in the initial phase of membrane proliferation. J. Cell Biol. 1974, 62:635-646.
    • (1974) J. Cell Biol. , vol.62 , pp. 635-646
    • Higgins, J.A.1
  • 25
    • 39149109255 scopus 로고    scopus 로고
    • Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data
    • Lavoie C., Paiement J. Topology of molecular machines of the endoplasmic reticulum: a compilation of proteomics and cytological data. Histochem. Cell Biol. 2008, 129:117-128.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 117-128
    • Lavoie, C.1    Paiement, J.2
  • 26
    • 12844286809 scopus 로고    scopus 로고
    • Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates
    • Gilham D., Alam M., Gao W., Vance D.E., Lehner R. Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates. Mol. Biol. Cell 2005, 16:984-996.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 984-996
    • Gilham, D.1    Alam, M.2    Gao, W.3    Vance, D.E.4    Lehner, R.5
  • 27
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel M.J., Hom E.F., Verkman A.S. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 1999, 76:2843-2851.
    • (1999) Biophys. J. , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.2    Verkman, A.S.3
  • 28
    • 1242349907 scopus 로고    scopus 로고
    • Kinesin dependent, rapid, bi-directional transport of ER sub-compartment in dendrites of hippocampal neurons
    • Bannai H., Inoue T., Nakayama T., Hattori M., Mikoshiba K. Kinesin dependent, rapid, bi-directional transport of ER sub-compartment in dendrites of hippocampal neurons. J. Cell Sci. 2004, 117:163-175.
    • (2004) J. Cell Sci. , vol.117 , pp. 163-175
    • Bannai, H.1    Inoue, T.2    Nakayama, T.3    Hattori, M.4    Mikoshiba, K.5
  • 29
  • 31
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Shibata Y., Voss C., Rist J.M., Hu J., Rapoport T.A., Prinz W.A., Voeltz G.K. The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J. Biol. Chem. 2008, 283:18892-18904.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6    Voeltz, G.K.7
  • 34
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: a dynamic gateway at the ER membrane
    • Johnson A.E., van Waes M.A. The translocon: a dynamic gateway at the ER membrane. Annu. Rev. Cell Dev. Biol. 1999, 15:799-842.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    van Waes, M.A.2
  • 36
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex
    • Kalies K.U., Gorlich D., Rapoport T.A. Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J. Cell Biol. 1994, 126:925-934.
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.U.1    Gorlich, D.2    Rapoport, T.A.3
  • 37
    • 42949117285 scopus 로고    scopus 로고
    • Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells
    • Stephens S.B., Dodd R.D., Lerner R.S., Pyhtila B.M., Nicchitta C.V. Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells. Methods Mol. Biol. 2008, 419:197-214.
    • (2008) Methods Mol. Biol. , vol.419 , pp. 197-214
    • Stephens, S.B.1    Dodd, R.D.2    Lerner, R.S.3    Pyhtila, B.M.4    Nicchitta, C.V.5
  • 38
    • 61949239472 scopus 로고    scopus 로고
    • Knockdown of p180 eliminates the terminal differentiation of a secretory cell line
    • Benyamini P., Webster P., Meyer D.I. Knockdown of p180 eliminates the terminal differentiation of a secretory cell line. Mol. Biol. Cell 2009, 20:732-744.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 732-744
    • Benyamini, P.1    Webster, P.2    Meyer, D.I.3
  • 39
    • 17044419154 scopus 로고    scopus 로고
    • Targeting proteins to membranes: structure of the signal recognition particle
    • Egea P.F., Stroud R.M., Walter P. Targeting proteins to membranes: structure of the signal recognition particle. Curr. Opin. Struct. Biol. 2005, 15:213-220.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 213-220
    • Egea, P.F.1    Stroud, R.M.2    Walter, P.3
  • 40
    • 0041977048 scopus 로고    scopus 로고
    • Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum
    • Mandon E.C., Jiang Y., Gilmore R. Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum. J. Cell Biol. 2003, 162:575-585.
    • (2003) J. Cell Biol. , vol.162 , pp. 575-585
    • Mandon, E.C.1    Jiang, Y.2    Gilmore, R.3
  • 41
    • 33646168487 scopus 로고    scopus 로고
    • MRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation
    • Lerner R.S., Nicchitta C.V. mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation. RNA 2006, 12:775-789.
    • (2006) RNA , vol.12 , pp. 775-789
    • Lerner, R.S.1    Nicchitta, C.V.2
  • 42
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
    • Pyhtila B., Zheng T., Lager P.J., Keene J.D., Reedy M.C., Nicchitta C.V. Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum. RNA 2008, 14:445-453.
    • (2008) RNA , vol.14 , pp. 445-453
    • Pyhtila, B.1    Zheng, T.2    Lager, P.J.3    Keene, J.D.4    Reedy, M.C.5    Nicchitta, C.V.6
  • 44
    • 20744441520 scopus 로고    scopus 로고
    • Subunits of the translocon interact with components of the oligosaccharyl transferase complex
    • Chavan M., Yan A., Lennarz W.J. Subunits of the translocon interact with components of the oligosaccharyl transferase complex. J. Biol. Chem. 2005, 280:22917-22924.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22917-22924
    • Chavan, M.1    Yan, A.2    Lennarz, W.J.3
  • 45
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol. Cell 2003, 12:101-111.
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.J.1    Karaoglu, D.2    Mandon, E.C.3    Gilmore, R.4
  • 46
    • 17644366824 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
    • Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R. Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry 2005, 44:5982-5992.
    • (2005) Biochemistry , vol.44 , pp. 5982-5992
    • Shibatani, T.1    David, L.L.2    McCormack, A.L.3    Frueh, K.4    Skach, W.R.5
  • 47
    • 66349084131 scopus 로고    scopus 로고
    • Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site
    • Harada Y., Li H., Lennarz W.J. Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site. Proc. Natl. Acad. Sci. USA 2009, 106:6945-6949.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6945-6949
    • Harada, Y.1    Li, H.2    Lennarz, W.J.3
  • 48
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada C., Kelleher D.J., Gilmore R. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 2009, 136:272-283.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 50
    • 0034635564 scopus 로고    scopus 로고
    • Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum
    • Fu J., Kreibich G. Retention of subunits of the oligosaccharyltransferase complex in the endoplasmic reticulum. J. Biol. Chem. 2000, 275:3984-3990.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3984-3990
    • Fu, J.1    Kreibich, G.2
  • 52
    • 33751185584 scopus 로고    scopus 로고
    • Protein transport into the endoplasmic reticulum: mechanisms and pathologies
    • Zimmermann R., Muller L., Wullich B. Protein transport into the endoplasmic reticulum: mechanisms and pathologies. Trends Mol. Med. 2006, 12:567-573.
    • (2006) Trends Mol. Med. , vol.12 , pp. 567-573
    • Zimmermann, R.1    Muller, L.2    Wullich, B.3
  • 53
    • 14944361914 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus
    • Wang X., Johnsson N. Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus. J. Cell Sci. 2005, 118:723-732.
    • (2005) J. Cell Sci. , vol.118 , pp. 723-732
    • Wang, X.1    Johnsson, N.2
  • 54
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen T., Lynes E.M., Gesson K., Thomas G. Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim. Biophys. Acta 2010, 1798:1465-1473.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 55
    • 13444271726 scopus 로고    scopus 로고
    • The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum
    • Alder N.N., Shen Y., Brodsky J.L., Hendershot L.M., Johnson A.E. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J. Cell Biol. 2005, 168:389-399.
    • (2005) J. Cell Biol. , vol.168 , pp. 389-399
    • Alder, N.N.1    Shen, Y.2    Brodsky, J.L.3    Hendershot, L.M.4    Johnson, A.E.5
  • 56
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh N.G., Johnson A.E. A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane. J. Cell Biol. 2002, 156:261-270.
    • (2002) J. Cell Biol. , vol.156 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 57
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman B.D., Hendershot L.M., Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 1998, 92:747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 58
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi A.K., Schekman R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 1997, 137:1483-1493.
    • (1997) J. Cell Biol. , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 59
    • 77950284301 scopus 로고    scopus 로고
    • Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction
    • Hayashi T., Fujimoto M. Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction. Mol. Pharmacol. 2010, 77:517-528.
    • (2010) Mol. Pharmacol. , vol.77 , pp. 517-528
    • Hayashi, T.1    Fujimoto, M.2
  • 60
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen W., Helenius J., Braakman I., Helenius A. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. USA 1995, 92:6229-6233.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 61
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U., Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 1997, 136:555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 66
    • 33847199803 scopus 로고    scopus 로고
    • Sheets, ribbons and tubules-how organelles get their shape
    • Voeltz G.K., Prinz W.A. Sheets, ribbons and tubules-how organelles get their shape. Nat. Rev. Mol. Cell Biol. 2007, 8:258-264.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 258-264
    • Voeltz, G.K.1    Prinz, W.A.2
  • 67
    • 77954218288 scopus 로고    scopus 로고
    • Further assembly required: construction and dynamics of the endoplasmic reticulum network
    • Park S.H., Blackstone C. Further assembly required: construction and dynamics of the endoplasmic reticulum network. EMBO Rep. 2010, 11:515-521.
    • (2010) EMBO Rep. , vol.11 , pp. 515-521
    • Park, S.H.1    Blackstone, C.2
  • 68
    • 34447519108 scopus 로고    scopus 로고
    • Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes
    • Nikonov A.V., Hauri H.P., Lauring B., Kreibich G. Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes. J. Cell Sci. 2007, 120:2248-2258.
    • (2007) J. Cell Sci. , vol.120 , pp. 2248-2258
    • Nikonov, A.V.1    Hauri, H.P.2    Lauring, B.3    Kreibich, G.4
  • 69
    • 34948905714 scopus 로고    scopus 로고
    • P180 is involved in the interaction between the endoplasmic reticulum and microtubules through a novel microtubule-binding and bundling domain
    • Ogawa-Goto K., Tanaka K., Ueno T., Kurata T., Sata T., Irie S. p180 is involved in the interaction between the endoplasmic reticulum and microtubules through a novel microtubule-binding and bundling domain. Mol. Biol. Cell 2007, 18:3741-3751.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3741-3751
    • Ogawa-Goto, K.1    Tanaka, K.2    Ueno, T.3    Kurata, T.4    Sata, T.5    Irie, S.6
  • 70
    • 77956934887 scopus 로고    scopus 로고
    • Enhancement of procollagen biosynthesis by p180 through augmented ribosome association on the endoplasmic reticulum in response to stimulated secretion
    • Ueno T., Tanaka K., Kaneko K., Taga Y., Sata T., Irie S., Hattori S., Ogawa-Goto K. Enhancement of procollagen biosynthesis by p180 through augmented ribosome association on the endoplasmic reticulum in response to stimulated secretion. J. Biol. Chem. 2010, 285:29941-29950.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29941-29950
    • Ueno, T.1    Tanaka, K.2    Kaneko, K.3    Taga, Y.4    Sata, T.5    Irie, S.6    Hattori, S.7    Ogawa-Goto, K.8
  • 72
    • 41449111412 scopus 로고    scopus 로고
    • Building and operating an antibody factory: redox control during B to plasma cell terminal differentiation
    • Masciarelli S., Sitia R. Building and operating an antibody factory: redox control during B to plasma cell terminal differentiation. Biochim. Biophys. Acta 2008, 1783:578-588.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 578-588
    • Masciarelli, S.1    Sitia, R.2
  • 74
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L., Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 1988, 4:335-374.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 75
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane
    • Dreger M., Bengtsson L., Schoneberg T., Otto H., Hucho F. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc. Natl. Acad. Sci. USA 2001, 98:11943-11948.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schoneberg, T.3    Otto, H.4    Hucho, F.5
  • 76
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer E.C., Florens L., Guan T., Yates J.R., Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 2003, 301:1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 77
    • 34848870027 scopus 로고    scopus 로고
    • Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum
    • Anderson D.J., Hetzer M.W. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nat. Cell Biol. 2007, 9:1160-1166.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1160-1166
    • Anderson, D.J.1    Hetzer, M.W.2
  • 78
    • 59149091333 scopus 로고    scopus 로고
    • Inner nuclear membrane protein transport is mediated by multiple mechanisms
    • Zuleger N., Korfali N., Schirmer E.C. Inner nuclear membrane protein transport is mediated by multiple mechanisms. Biochem. Soc. Trans. 2008, 36:1373-1377.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1373-1377
    • Zuleger, N.1    Korfali, N.2    Schirmer, E.C.3
  • 81
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • Starr D.A., Fridolfsson H.N. Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu. Rev. Cell Dev. Biol. 2010, 26:421-444.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 83
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M., Trembath R.C., Shackleton S. SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol. Cell. Biol. 2006, 26:3738-3751.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Trembath, R.C.7    Shackleton, S.8
  • 84
    • 35648937494 scopus 로고    scopus 로고
    • Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin
    • Ketema M., Wilhelmsen K., Kuikman I., Janssen H., Hodzic D., Sonnenberg A. Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. J. Cell Sci. 2007, 120:3384-3394.
    • (2007) J. Cell Sci. , vol.120 , pp. 3384-3394
    • Ketema, M.1    Wilhelmsen, K.2    Kuikman, I.3    Janssen, H.4    Hodzic, D.5    Sonnenberg, A.6
  • 89
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz G.K., Prinz W.A., Shibata Y., Rist J.M., Rapoport T.A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 2006, 124:573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 90
    • 40449124075 scopus 로고    scopus 로고
    • The reticulons: a family of proteins with diverse functions
    • Yang Y.S., Strittmatter S.M. The reticulons: a family of proteins with diverse functions. Genome Biol. 2007, 8:234.
    • (2007) Genome Biol. , vol.8 , pp. 234
    • Yang, Y.S.1    Strittmatter, S.M.2
  • 91
    • 33847164931 scopus 로고    scopus 로고
    • Two hydrophobic segments of the RTN1 family determine the ER localization and retention
    • Iwahashi J., Hamada N., Watanabe H. Two hydrophobic segments of the RTN1 family determine the ER localization and retention. Biochem. Biophys. Res. Commun. 2007, 355:508-512.
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 508-512
    • Iwahashi, J.1    Hamada, N.2    Watanabe, H.3
  • 92
    • 35148885295 scopus 로고    scopus 로고
    • Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth
    • Kiseleva E., Morozova K.N., Voeltz G.K., Allen T.D., Goldberg M.W. Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth. J. Struct. Biol. 2007, 160:224-235.
    • (2007) J. Struct. Biol. , vol.160 , pp. 224-235
    • Kiseleva, E.1    Morozova, K.N.2    Voeltz, G.K.3    Allen, T.D.4    Goldberg, M.W.5
  • 95
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 96
    • 0032734577 scopus 로고    scopus 로고
    • The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells
    • Pitts K.R., Yoon Y., Krueger E.W., McNiven M.A. The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Mol. Biol. Cell 1999, 10:4403-4417.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4403-4417
    • Pitts, K.R.1    Yoon, Y.2    Krueger, E.W.3    McNiven, M.A.4
  • 98
    • 21644459401 scopus 로고    scopus 로고
    • Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane
    • Ozeki S., Cheng J., Tauchi-Sato K., Hatano N., Taniguchi H., Fujimoto T. Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane. J. Cell Sci. 2005, 118:2601-2611.
    • (2005) J. Cell Sci. , vol.118 , pp. 2601-2611
    • Ozeki, S.1    Cheng, J.2    Tauchi-Sato, K.3    Hatano, N.4    Taniguchi, H.5    Fujimoto, T.6
  • 99
    • 34347385833 scopus 로고    scopus 로고
    • A role for Rab5 in structuring the endoplasmic reticulum
    • Audhya A., Desai A., Oegema K. A role for Rab5 in structuring the endoplasmic reticulum. J. Cell Biol. 2007, 178:43-56.
    • (2007) J. Cell Biol. , vol.178 , pp. 43-56
    • Audhya, A.1    Desai, A.2    Oegema, K.3
  • 100
    • 0016242035 scopus 로고
    • Localization of calcium in the smooth endoplasmic reticulum of rat isolated fat cells
    • Hales C.N., Luzio J.P., Chandler J.A., Herman L. Localization of calcium in the smooth endoplasmic reticulum of rat isolated fat cells. J. Cell Sci. 1974, 15:1-15.
    • (1974) J. Cell Sci. , vol.15 , pp. 1-15
    • Hales, C.N.1    Luzio, J.P.2    Chandler, J.A.3    Herman, L.4
  • 101
    • 0019307667 scopus 로고
    • Localization of calcium in presynaptic nerve terminals, an ultrastructural and electron microprobe analysis
    • McGraw C.F., Somlyo A.V., Blaustein M.P. Localization of calcium in presynaptic nerve terminals, an ultrastructural and electron microprobe analysis. J. Cell Biol. 1980, 85:228-241.
    • (1980) J. Cell Biol. , vol.85 , pp. 228-241
    • McGraw, C.F.1    Somlyo, A.V.2    Blaustein, M.P.3
  • 102
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells
    • Pezzati R., Bossi M., Podini P., Meldolesi J., Grohovaz F. High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozen-freeze dried PC12 cells. Mol. Biol. Cell 1997, 8:1501-1512.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 103
    • 0025359122 scopus 로고
    • The inositol 1,4,5,-trisphosphate receptor in cerebellar Purkinje cells: quantitative immunogold labeling reveals concentration in an ER subcompartment
    • Satoh T., Ross C.A., Villa A., Supattapone S., Pozzan T., Snyder S.H., Meldolesi J. The inositol 1,4,5,-trisphosphate receptor in cerebellar Purkinje cells: quantitative immunogold labeling reveals concentration in an ER subcompartment. J. Cell Biol. 1990, 111:615-624.
    • (1990) J. Cell Biol. , vol.111 , pp. 615-624
    • Satoh, T.1    Ross, C.A.2    Villa, A.3    Supattapone, S.4    Pozzan, T.5    Snyder, S.H.6    Meldolesi, J.7
  • 104
    • 0026610662 scopus 로고
    • Ca2+ stores in Purkinje neurons: endoplasmic reticulum subcompartments demonstrated by the heterogeneous distribution of the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin
    • Takei K., Stukenbrok H., Metcalf A., Mignery G.A., Sudhof T.C., Volpe P., De Camilli P. Ca2+ stores in Purkinje neurons: endoplasmic reticulum subcompartments demonstrated by the heterogeneous distribution of the InsP3 receptor, Ca(2+)-ATPase, and calsequestrin. J. Neurosci. 1992, 12:489-505.
    • (1992) J. Neurosci. , vol.12 , pp. 489-505
    • Takei, K.1    Stukenbrok, H.2    Metcalf, A.3    Mignery, G.A.4    Sudhof, T.C.5    Volpe, P.6    De Camilli, P.7
  • 105
    • 0029850426 scopus 로고    scopus 로고
    • The endoplasmic reticulum in PC12 cells. Evidence for a mosaic of domains differently specialized in Ca2+ handling
    • Rooney E., Meldolesi J. The endoplasmic reticulum in PC12 cells. Evidence for a mosaic of domains differently specialized in Ca2+ handling. J. Biol. Chem. 1996, 271:29304-29311.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29304-29311
    • Rooney, E.1    Meldolesi, J.2
  • 106
    • 0030999715 scopus 로고    scopus 로고
    • Spatially and functionally distinct Ca2+ stores in sarcoplasmic and endoplasmic reticulum
    • Golovina V.A., Blaustein M.P. Spatially and functionally distinct Ca2+ stores in sarcoplasmic and endoplasmic reticulum. Science 1997, 275:1643-1648.
    • (1997) Science , vol.275 , pp. 1643-1648
    • Golovina, V.A.1    Blaustein, M.P.2
  • 107
    • 0030611668 scopus 로고    scopus 로고
    • Ca2+ homeostasis in the endoplasmic reticulum: coexistence of high and low [Ca2+] subcompartments in intact HeLa cells
    • Montero M., Alvarez J., Scheenen W.J., Rizzuto R., Meldolesi J., Pozzan T. Ca2+ homeostasis in the endoplasmic reticulum: coexistence of high and low [Ca2+] subcompartments in intact HeLa cells. J. Cell Biol. 1997, 139:601-611.
    • (1997) J. Cell Biol. , vol.139 , pp. 601-611
    • Montero, M.1    Alvarez, J.2    Scheenen, W.J.3    Rizzuto, R.4    Meldolesi, J.5    Pozzan, T.6
  • 108
    • 0035341345 scopus 로고    scopus 로고
    • The endoplasmic reticulum: one continuous or several separate Ca(2+) stores?
    • Petersen O.H., Tepikin A., Park M.K. The endoplasmic reticulum: one continuous or several separate Ca(2+) stores?. Trends Neurosci. 2001, 24:271-276.
    • (2001) Trends Neurosci. , vol.24 , pp. 271-276
    • Petersen, O.H.1    Tepikin, A.2    Park, M.K.3
  • 111
    • 70350012303 scopus 로고    scopus 로고
    • Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells
    • Wieckowski M.R., Giorgi C., Lebiedzinska M., Duszynski J., Pinton P. Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells. Nat. Protoc. 2009, 4:1582-1590.
    • (2009) Nat. Protoc. , vol.4 , pp. 1582-1590
    • Wieckowski, M.R.1    Giorgi, C.2    Lebiedzinska, M.3    Duszynski, J.4    Pinton, P.5
  • 112
    • 0038106252 scopus 로고    scopus 로고
    • The type 3 inositol 1,4,5-trisphosphate receptor is concentrated at the tight junction level in polarized MDCK cells
    • Colosetti P., Tunwell R.E., Cruttwell C., Arsanto J.P., Mauger J.P., Cassio D. The type 3 inositol 1,4,5-trisphosphate receptor is concentrated at the tight junction level in polarized MDCK cells. J. Cell Sci. 2003, 116:2791-2803.
    • (2003) J. Cell Sci. , vol.116 , pp. 2791-2803
    • Colosetti, P.1    Tunwell, R.E.2    Cruttwell, C.3    Arsanto, J.P.4    Mauger, J.P.5    Cassio, D.6
  • 113
    • 0032555788 scopus 로고    scopus 로고
    • The heterogeneity of ER Ca2+ stores has a key role in nonmuscle cell signaling and function
    • Meldolesi J., Pozzan T. The heterogeneity of ER Ca2+ stores has a key role in nonmuscle cell signaling and function. J. Cell Biol. 1998, 142:1395-1398.
    • (1998) J. Cell Biol. , vol.142 , pp. 1395-1398
    • Meldolesi, J.1    Pozzan, T.2
  • 114
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi T., Su T.P. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 2007, 131:596-610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 115
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li G., Mongillo M., Chin K.T., Harding H., Ron D., Marks A.R., Tabas I. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J. Cell Biol. 2009, 186:783-792.
    • (2009) J. Cell Biol. , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6    Tabas, I.7
  • 116
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+-dependent redox modulation of SERCA 2b by ERp57
    • Li Y., Camacho P. Ca2+-dependent redox modulation of SERCA 2b by ERp57. J. Cell Biol. 2004, 164:35-46.
    • (2004) J. Cell Biol. , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 117
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b
    • Roderick H.L., Lechleiter J.D., Camacho P. Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b. J. Cell Biol. 2000, 149:1235-1248.
    • (2000) J. Cell Biol. , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 118
    • 11844269232 scopus 로고    scopus 로고
    • Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44
    • Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 2005, 120:85-98.
    • (2005) Cell , vol.120 , pp. 85-98
    • Higo, T.1    Hattori, M.2    Nakamura, T.3    Natsume, T.4    Michikawa, T.5    Mikoshiba, K.6
  • 119
    • 77955708533 scopus 로고    scopus 로고
    • Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM)
    • Gilady S.Y., Bui M., Lynes E.M., Benson M.D., Watts R., Vance J.E., Simmen T. Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress Chaperones 2010, 15:619-629.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 619-629
    • Gilady, S.Y.1    Bui, M.2    Lynes, E.M.3    Benson, M.D.4    Watts, R.5    Vance, J.E.6    Simmen, T.7
  • 122
    • 4344699902 scopus 로고    scopus 로고
    • Calreticulin, Ca2+, and calcineurin-signaling from the endoplasmic reticulum
    • Groenendyk J., Lynch J., Michalak M. Calreticulin, Ca2+, and calcineurin-signaling from the endoplasmic reticulum. Mol. Cells 2004, 17:383-389.
    • (2004) Mol. Cells , vol.17 , pp. 383-389
    • Groenendyk, J.1    Lynch, J.2    Michalak, M.3
  • 123
    • 0025923376 scopus 로고
    • Intracellular Ca2+ stores in chicken Purkinje neurons: differential distribution of the low affinity-high capacity Ca2+ binding protein, calsequestrin, of Ca2+ ATPase and of the ER lumenal protein, Bip
    • Villa A., Podini P., Clegg D.O., Pozzan T., Meldolesi J. Intracellular Ca2+ stores in chicken Purkinje neurons: differential distribution of the low affinity-high capacity Ca2+ binding protein, calsequestrin, of Ca2+ ATPase and of the ER lumenal protein, Bip. J. Cell Biol. 1991, 113:779-791.
    • (1991) J. Cell Biol. , vol.113 , pp. 779-791
    • Villa, A.1    Podini, P.2    Clegg, D.O.3    Pozzan, T.4    Meldolesi, J.5
  • 125
    • 0035817628 scopus 로고    scopus 로고
    • Head-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of endoplasmic reticulum luminal proteins
    • Gatti G., Trifari S., Mesaeli N., Parker J.M., Michalak M., Meldolesi J. Head-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of endoplasmic reticulum luminal proteins. J. Cell Biol. 2001, 154:525-534.
    • (2001) J. Cell Biol. , vol.154 , pp. 525-534
    • Gatti, G.1    Trifari, S.2    Mesaeli, N.3    Parker, J.M.4    Michalak, M.5    Meldolesi, J.6
  • 126
    • 77956172122 scopus 로고    scopus 로고
    • Rough endoplasmic reticulum to junctional sarcoplasmic reticulum trafficking of calsequestrin in adult cardiomyocytes
    • McFarland T.P., Milstein M.L., Cala S.E. Rough endoplasmic reticulum to junctional sarcoplasmic reticulum trafficking of calsequestrin in adult cardiomyocytes. J. Mol. Cell. Cardiol. 2010, 49:556-564.
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 556-564
    • McFarland, T.P.1    Milstein, M.L.2    Cala, S.E.3
  • 127
    • 0017174781 scopus 로고
    • The endoplasmic reticulum: a cytochemist's view (a review)
    • Novikoff A.B. The endoplasmic reticulum: a cytochemist's view (a review). Proc. Natl. Acad. Sci. USA 1976, 73:2781-2787.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2781-2787
    • Novikoff, A.B.1
  • 128
    • 0009634379 scopus 로고
    • Lysosomal compartment of macrophages: extending the definition of GERL
    • Novikoff P.M., Yam A., Novikoff A.B. Lysosomal compartment of macrophages: extending the definition of GERL. Proc. Natl. Acad. Sci. USA 1981, 78:5699-5703.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5699-5703
    • Novikoff, P.M.1    Yam, A.2    Novikoff, A.B.3
  • 129
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi C., De Stefani D., Bononi A., Rizzuto R., Pinton P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 2009, 41:1817-1827.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 130
    • 33745444732 scopus 로고    scopus 로고
    • Interaction of the smooth endoplasmic reticulum and mitochondria
    • Goetz J.G., Nabi I.R. Interaction of the smooth endoplasmic reticulum and mitochondria. Biochem. Soc. Trans. 2006, 34:370-373.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 370-373
    • Goetz, J.G.1    Nabi, I.R.2
  • 131
    • 0034683749 scopus 로고    scopus 로고
    • Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum
    • Wang H.J., Guay G., Pogan L., Sauve R., Nabi I.R. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J. Cell Biol. 2000, 150:1489-1498.
    • (2000) J. Cell Biol. , vol.150 , pp. 1489-1498
    • Wang, H.J.1    Guay, G.2    Pogan, L.3    Sauve, R.4    Nabi, I.R.5
  • 132
    • 0021340291 scopus 로고
    • Isolation of plasma membrane, golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver
    • Croze E.M., Morre D.J. Isolation of plasma membrane, golgi apparatus, and endoplasmic reticulum fractions from single homogenates of mouse liver. J. Cell. Physiol. 1984, 119:46-57.
    • (1984) J. Cell. Physiol. , vol.119 , pp. 46-57
    • Croze, E.M.1    Morre, D.J.2
  • 133
    • 0015610440 scopus 로고
    • Ultrastructural morphometry of the pancreatic -cell
    • Dean P.M. Ultrastructural morphometry of the pancreatic -cell. Diabetologia 1973, 9:115-119.
    • (1973) Diabetologia , vol.9 , pp. 115-119
    • Dean, P.M.1
  • 135
    • 0344966647 scopus 로고
    • An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost
    • Copeland D.E., Dalton A.J. An association between mitochondria and the endoplasmic reticulum in cells of the pseudobranch gland of a teleost. J. Biophys. Biochem. Cytol. 1959, 5:393-396.
    • (1959) J. Biophys. Biochem. Cytol. , vol.5 , pp. 393-396
    • Copeland, D.E.1    Dalton, A.J.2
  • 137
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance J.E. Phospholipid synthesis in a membrane fraction associated with mitochondria. J. Biol. Chem. 1990, 265:7248-7256.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 138
    • 0027973135 scopus 로고
    • A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins
    • Rusinol A.E., Cui Z., Chen M.H., Vance J.E. A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins. J. Biol. Chem. 1994, 269:27494-27502.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27494-27502
    • Rusinol, A.E.1    Cui, Z.2    Chen, M.H.3    Vance, J.E.4
  • 140
    • 0037102527 scopus 로고    scopus 로고
    • Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and mitochondrial-associated membrane
    • Lewin T.M., Van Horn C.G., Krisans S.K., Coleman R.A. Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and mitochondrial-associated membrane. Arch. Biochem. Biophys. 2002, 404:263-270.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 263-270
    • Lewin, T.M.1    Van Horn, C.G.2    Krisans, S.K.3    Coleman, R.A.4
  • 141
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C., Voelker D.R., Langer T. Making heads or tails of phospholipids in mitochondria. J. Cell Biol. 2011, 192:7-16.
    • (2011) J. Cell Biol. , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 142
    • 64149132208 scopus 로고    scopus 로고
    • The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria
    • Stone S.J., Levin M.C., Zhou P., Han J., Walther T.C., Farese R.V. The endoplasmic reticulum enzyme DGAT2 is found in mitochondria-associated membranes and has a mitochondrial targeting signal that promotes its association with mitochondria. J. Biol. Chem. 2009, 284:5352-5361.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5352-5361
    • Stone, S.J.1    Levin, M.C.2    Zhou, P.3    Han, J.4    Walther, T.C.5    Farese, R.V.6
  • 143
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner G., Gaigg B., Krasser A., Kainersdorfer E., Kohlwein S.D., Perktold A., Zellnig G., Daum G. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 1999, 264:545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1    Gaigg, B.2    Krasser, A.3    Kainersdorfer, E.4    Kohlwein, S.D.5    Perktold, A.6    Zellnig, G.7    Daum, G.8
  • 144
    • 0026088027 scopus 로고
    • Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum
    • Vance J.E. Newly made phosphatidylserine and phosphatidylethanolamine are preferentially translocated between rat liver mitochondria and endoplasmic reticulum. J. Biol. Chem. 1991, 266:89-97.
    • (1991) J. Biol. Chem. , vol.266 , pp. 89-97
    • Vance, J.E.1
  • 145
    • 0344392841 scopus 로고    scopus 로고
    • A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery
    • Boldogh I.R., Nowakowski D.W., Yang H.C., Chung H., Karmon S., Royes P., Pon L.A. A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery. Mol. Biol. Cell 2003, 14:4618-4627.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.C.3    Chung, H.4    Karmon, S.5    Royes, P.6    Pon, L.A.7
  • 147
    • 33644905848 scopus 로고    scopus 로고
    • Diverse membrane-associated proteins contain a novel SMP domain
    • Lee I., Hong W. Diverse membrane-associated proteins contain a novel SMP domain. FASEB J. 2006, 20:202-206.
    • (2006) FASEB J. , vol.20 , pp. 202-206
    • Lee, I.1    Hong, W.2
  • 148
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D., Patterson R.L., Sedaghat L., Glebova N.O., Kurosaki T., Snyder S.H. Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat. Cell Biol. 2003, 5:1051-1061.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 152
    • 79551600416 scopus 로고    scopus 로고
    • Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction
    • Iwasawa R., Mahul-Mellier A.L., Datler C., Pazarentzos E., Grimm S. Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction. EMBO J. 2011, 30:556-568.
    • (2011) EMBO J. , vol.30 , pp. 556-568
    • Iwasawa, R.1    Mahul-Mellier, A.L.2    Datler, C.3    Pazarentzos, E.4    Grimm, S.5
  • 153
    • 69249213354 scopus 로고    scopus 로고
    • The COPI system: molecular mechanisms and function
    • Beck R., Rawet M., Wieland F.T., Cassel D. The COPI system: molecular mechanisms and function. FEBS Lett. 2009, 583:2701-2709.
    • (2009) FEBS Lett. , vol.583 , pp. 2701-2709
    • Beck, R.1    Rawet, M.2    Wieland, F.T.3    Cassel, D.4
  • 154
    • 77956334107 scopus 로고    scopus 로고
    • Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum
    • Tavender T.J., Bulleid N.J. Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid. Redox Signal. 2010, 13:1177-1187.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1177-1187
    • Tavender, T.J.1    Bulleid, N.J.2
  • 155
    • 77952296476 scopus 로고    scopus 로고
    • Cholesterol at the endoplasmic reticulum: roles of the sigma-1 receptor chaperone and implications thereof in human diseases
    • Hayashi T., Su T.P. Cholesterol at the endoplasmic reticulum: roles of the sigma-1 receptor chaperone and implications thereof in human diseases. Subcell. Biochem. 2010, 51:381-398.
    • (2010) Subcell. Biochem. , vol.51 , pp. 381-398
    • Hayashi, T.1    Su, T.P.2
  • 156
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman D.T., Resek M.E., Zajchowski L.D., Robbins S.M. Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J. Cell Sci. 2006, 119:3149-3160.
    • (2006) J. Cell Sci. , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 157
    • 33644982350 scopus 로고    scopus 로고
    • Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum
    • Campana V., Sarnataro D., Fasano C., Casanova P., Paladino S., Zurzolo C. Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum. J. Cell Sci. 2006, 119:433-442.
    • (2006) J. Cell Sci. , vol.119 , pp. 433-442
    • Campana, V.1    Sarnataro, D.2    Fasano, C.3    Casanova, P.4    Paladino, S.5    Zurzolo, C.6
  • 158
    • 42949089081 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases involved in ganglioside biosynthesis
    • van Echten-Deckert G., Gurgui M. Golgi localization of glycosyltransferases involved in ganglioside biosynthesis. Curr. Drug Targets 2008, 9:282-291.
    • (2008) Curr. Drug Targets , vol.9 , pp. 282-291
    • van Echten-Deckert, G.1    Gurgui, M.2
  • 159
    • 70449088871 scopus 로고    scopus 로고
    • GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2+)-dependent mitochondrial apoptosis
    • Sano R., Annunziata I., Patterson A., Moshiach S., Gomero E., Opferman J., Forte M., d'Azzo A. GM1-ganglioside accumulation at the mitochondria-associated ER membranes links ER stress to Ca(2+)-dependent mitochondrial apoptosis. Mol. Cell 2009, 36:500-511.
    • (2009) Mol. Cell , vol.36 , pp. 500-511
    • Sano, R.1    Annunziata, I.2    Patterson, A.3    Moshiach, S.4    Gomero, E.5    Opferman, J.6    Forte, M.7    d'Azzo, A.8
  • 160
    • 0037924355 scopus 로고    scopus 로고
    • Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export
    • Hayashi T., Su T.P. Sigma-1 receptors (sigma(1) binding sites) form raft-like microdomains and target lipid droplets on the endoplasmic reticulum: roles in endoplasmic reticulum lipid compartmentalization and export. J. Pharmacol. Exp. Ther. 2003, 306:718-725.
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 718-725
    • Hayashi, T.1    Su, T.P.2
  • 161
    • 0014533030 scopus 로고
    • Isolation of rough and smooth microsomes from rat liver by means of a commerically available centrifuge
    • Bergstrand A., Dallner G. Isolation of rough and smooth microsomes from rat liver by means of a commerically available centrifuge. Anal. Biochem. 1969, 29:351-356.
    • (1969) Anal. Biochem. , vol.29 , pp. 351-356
    • Bergstrand, A.1    Dallner, G.2
  • 162
    • 56449110891 scopus 로고    scopus 로고
    • Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance
    • Radhakrishnan A., Goldstein J.L., McDonald J.G., Brown M.S. Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance. Cell Metab. 2008, 8:512-521.
    • (2008) Cell Metab. , vol.8 , pp. 512-521
    • Radhakrishnan, A.1    Goldstein, J.L.2    McDonald, J.G.3    Brown, M.S.4
  • 163
    • 0035448312 scopus 로고    scopus 로고
    • A role for smooth endoplasmic reticulum membrane cholesterol ester in determining the intracellular location and regulation of sterol-regulatory-element-binding protein-2
    • Iddon C.R., Wilkinson J., Bennett A.J., Bennett J., Salter A.M., Higgins J.A. A role for smooth endoplasmic reticulum membrane cholesterol ester in determining the intracellular location and regulation of sterol-regulatory-element-binding protein-2. Biochem. J. 2001, 358:415-422.
    • (2001) Biochem. J. , vol.358 , pp. 415-422
    • Iddon, C.R.1    Wilkinson, J.2    Bennett, A.J.3    Bennett, J.4    Salter, A.M.5    Higgins, J.A.6
  • 164
    • 0030474081 scopus 로고    scopus 로고
    • Cell compartmentalization of cholesterol biosynthesis
    • Krisans S.K. Cell compartmentalization of cholesterol biosynthesis. Ann. N. Y. Acad. Sci. 1996, 804:142-164.
    • (1996) Ann. N. Y. Acad. Sci. , vol.804 , pp. 142-164
    • Krisans, S.K.1
  • 165
    • 37049016678 scopus 로고    scopus 로고
    • Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines
    • Palmer C.P., Mahen R., Schnell E., Djamgoz M.B., Aydar E. Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines. Cancer Res. 2007, 67:11166-11175.
    • (2007) Cancer Res. , vol.67 , pp. 11166-11175
    • Palmer, C.P.1    Mahen, R.2    Schnell, E.3    Djamgoz, M.B.4    Aydar, E.5
  • 166
    • 4344578601 scopus 로고    scopus 로고
    • Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: implications for depletion of endoplasmic reticulum calcium stores and apoptosis in cholesterol-loaded macrophages
    • Li Y., Ge M., Ciani L., Kuriakose G., Westover E.J., Dura M., Covey D.F., Freed J.H., Maxfield F.R., Lytton J., Tabas I. Enrichment of endoplasmic reticulum with cholesterol inhibits sarcoplasmic-endoplasmic reticulum calcium ATPase-2b activity in parallel with increased order of membrane lipids: implications for depletion of endoplasmic reticulum calcium stores and apoptosis in cholesterol-loaded macrophages. J. Biol. Chem. 2004, 279:37030-37039.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37030-37039
    • Li, Y.1    Ge, M.2    Ciani, L.3    Kuriakose, G.4    Westover, E.J.5    Dura, M.6    Covey, D.F.7    Freed, J.H.8    Maxfield, F.R.9    Lytton, J.10    Tabas, I.11
  • 167
    • 70450225048 scopus 로고    scopus 로고
    • ER exit sites-localization and control of COPII vesicle formation
    • Budnik A., Stephens D.J. ER exit sites-localization and control of COPII vesicle formation. FEBS Lett. 2009, 583:3796-3803.
    • (2009) FEBS Lett. , vol.583 , pp. 3796-3803
    • Budnik, A.1    Stephens, D.J.2
  • 168
    • 15844406577 scopus 로고    scopus 로고
    • Exiting the endoplasmic reticulum
    • Mancias J.D., Goldberg J. Exiting the endoplasmic reticulum. Traffic 2005, 6:278-285.
    • (2005) Traffic , vol.6 , pp. 278-285
    • Mancias, J.D.1    Goldberg, J.2
  • 169
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh S.I., Rowe T., Balch W.E. The organization of endoplasmic reticulum export complexes. J. Cell Biol. 1996, 135:19-35.
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 170
  • 171
    • 33947104123 scopus 로고    scopus 로고
    • Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization
    • Bhattacharyya D., Glick B.S. Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization. Mol. Biol. Cell 2007, 18:839-849.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 839-849
    • Bhattacharyya, D.1    Glick, B.S.2
  • 172
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • Watson P., Townley A.K., Koka P., Palmer K.J., Stephens D.J. Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 2006, 7:1678-1687.
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 174
    • 57349165449 scopus 로고    scopus 로고
    • Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif
    • Ivan V., de Voer G., Xanthakis D., Spoorendonk K.M., Kondylis V., Rabouille C. Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif. Mol. Biol. Cell 2008, 19:4352-4365.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4352-4365
    • Ivan, V.1    de Voer, G.2    Xanthakis, D.3    Spoorendonk, K.M.4    Kondylis, V.5    Rabouille, C.6
  • 175
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C., Hauri H.P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 2006, 119:2173-2183.
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 176
    • 0027328703 scopus 로고
    • ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif
    • Schindler R., Itin C., Zerial M., Lottspeich F., Hauri H.P. ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif. Eur. J. Cell Biol. 1993, 61:1-9.
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 1-9
    • Schindler, R.1    Itin, C.2    Zerial, M.3    Lottspeich, F.4    Hauri, H.P.5
  • 177
    • 0029029563 scopus 로고
    • Trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention
    • Wahlberg J.M., Geffen I., Reymond F., Simmen T., Spiess M. trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention. J. Cell Biol. 1995, 130:285-297.
    • (1995) J. Cell Biol. , vol.130 , pp. 285-297
    • Wahlberg, J.M.1    Geffen, I.2    Reymond, F.3    Simmen, T.4    Spiess, M.5
  • 178
    • 42049097236 scopus 로고    scopus 로고
    • Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum
    • Ronchi P., Colombo S., Francolini M., Borgese N. Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum. J. Cell Biol. 2008, 181:105-118.
    • (2008) J. Cell Biol. , vol.181 , pp. 105-118
    • Ronchi, P.1    Colombo, S.2    Francolini, M.3    Borgese, N.4
  • 179
    • 44449107477 scopus 로고    scopus 로고
    • Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum
    • Abrami L., Kunz B., Iacovache I., van der Goot F.G. Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 2008, 105:5384-5389.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5384-5389
    • Abrami, L.1    Kunz, B.2    Iacovache, I.3    van der Goot, F.G.4
  • 180
  • 182
    • 22544466429 scopus 로고    scopus 로고
    • Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro
    • Sun L.P., Li L., Goldstein J.L., Brown M.S. Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro. J. Biol. Chem. 2005, 280:26483-26490.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26483-26490
    • Sun, L.P.1    Li, L.2    Goldstein, J.L.3    Brown, M.S.4
  • 183
    • 70350400757 scopus 로고    scopus 로고
    • The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage
    • Irisawa M., Inoue J., Ozawa N., Mori K., Sato R. The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage. J. Biol. Chem. 2009, 284:28995-29004.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28995-29004
    • Irisawa, M.1    Inoue, J.2    Ozawa, N.3    Mori, K.4    Sato, R.5
  • 184
    • 0035023874 scopus 로고    scopus 로고
    • A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids
    • Pichler H., Gaigg B., Hrastnik C., Achleitner G., Kohlwein S.D., Zellnig G., Perktold A., Daum G. A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids. Eur. J. Biochem. 2001, 268:2351-2361.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2351-2361
    • Pichler, H.1    Gaigg, B.2    Hrastnik, C.3    Achleitner, G.4    Kohlwein, S.D.5    Zellnig, G.6    Perktold, A.7    Daum, G.8
  • 186
    • 7244238074 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum
    • Li Y., Prinz W.A. ATP-binding cassette (ABC) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum. J. Biol. Chem. 2004, 279:45226-45234.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45226-45234
    • Li, Y.1    Prinz, W.A.2
  • 187
    • 0442292211 scopus 로고    scopus 로고
    • The exocyst meets the translocon: a regulatory circuit for secretion and protein synthesis?
    • Guo W., Novick P. The exocyst meets the translocon: a regulatory circuit for secretion and protein synthesis?. Trends Cell Biol. 2004, 14:61-63.
    • (2004) Trends Cell Biol. , vol.14 , pp. 61-63
    • Guo, W.1    Novick, P.2
  • 188
    • 0344875517 scopus 로고    scopus 로고
    • Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum
    • Wiederkehr A., Du Y., Pypaert M., Ferro-Novick S., Novick P. Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum. Mol. Biol. Cell 2003, 14:4770-4782.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4770-4782
    • Wiederkehr, A.1    Du, Y.2    Pypaert, M.3    Ferro-Novick, S.4    Novick, P.5
  • 189
    • 0037899298 scopus 로고    scopus 로고
    • The exocyst affects protein synthesis by acting on the translocation machinery of the endoplasmic reticulum
    • Lipschutz J.H., Lingappa V.R., Mostov K.E. The exocyst affects protein synthesis by acting on the translocation machinery of the endoplasmic reticulum. J. Biol. Chem. 2003, 278:20954-20960.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20954-20960
    • Lipschutz, J.H.1    Lingappa, V.R.2    Mostov, K.E.3
  • 190
    • 33947243452 scopus 로고    scopus 로고
    • The molecular choreography of a store-operated calcium channel
    • Lewis R.S. The molecular choreography of a store-operated calcium channel. Nature 2007, 446:284-287.
    • (2007) Nature , vol.446 , pp. 284-287
    • Lewis, R.S.1
  • 191
    • 68949192292 scopus 로고    scopus 로고
    • Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles
    • Lebiedzinska M., Szabadkai G., Jones A.W., Duszynski J., Wieckowski M.R. Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles. Int. J. Biochem. Cell Biol. 2009, 41:1805-1816.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1805-1816
    • Lebiedzinska, M.1    Szabadkai, G.2    Jones, A.W.3    Duszynski, J.4    Wieckowski, M.R.5
  • 192
    • 0032541025 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that precedes its externalization during programmed cell death
    • Aussel C., Pelassy C., Breittmayer J.P. CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that precedes its externalization during programmed cell death. FEBS Lett. 1998, 431:195-199.
    • (1998) FEBS Lett. , vol.431 , pp. 195-199
    • Aussel, C.1    Pelassy, C.2    Breittmayer, J.P.3
  • 193
    • 0034721547 scopus 로고    scopus 로고
    • Preferential externalization of newly synthesized phosphatidylserine in apoptotic U937 cells is dependent on caspase-mediated pathways
    • Yu A., Byers D.M., Ridgway N.D., McMaster C.R., Cook H.W. Preferential externalization of newly synthesized phosphatidylserine in apoptotic U937 cells is dependent on caspase-mediated pathways. Biochim. Biophys. Acta 2000, 1487:296-308.
    • (2000) Biochim. Biophys. Acta , vol.1487 , pp. 296-308
    • Yu, A.1    Byers, D.M.2    Ridgway, N.D.3    McMaster, C.R.4    Cook, H.W.5
  • 194
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok V.A., Voelker D.R., Campbell P.A., Cohen J.J., Bratton D.L., Henson P.M. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 1992, 148:2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 197
  • 198
    • 30044449332 scopus 로고    scopus 로고
    • Subplasmalemmal mitochondria modulate the activity of plasma membrane Ca2+-ATPases
    • Frieden M., Arnaudeau S., Castelbou C., Demaurex N. Subplasmalemmal mitochondria modulate the activity of plasma membrane Ca2+-ATPases. J. Biol. Chem. 2005, 280:43198-43208.
    • (2005) J. Biol. Chem. , vol.280 , pp. 43198-43208
    • Frieden, M.1    Arnaudeau, S.2    Castelbou, C.3    Demaurex, N.4
  • 199
    • 33748569838 scopus 로고    scopus 로고
    • Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane
    • Wu M.M., Buchanan J., Luik R.M., Lewis R.S. Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane. J. Cell Biol. 2006, 174:803-813.
    • (2006) J. Cell Biol. , vol.174 , pp. 803-813
    • Wu, M.M.1    Buchanan, J.2    Luik, R.M.3    Lewis, R.S.4
  • 201
    • 53149128421 scopus 로고    scopus 로고
    • Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry
    • Stathopulos P.B., Zheng L., Li G.Y., Plevin M.J., Ikura M. Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry. Cell 2008, 135:110-122.
    • (2008) Cell , vol.135 , pp. 110-122
    • Stathopulos, P.B.1    Zheng, L.2    Li, G.Y.3    Plevin, M.J.4    Ikura, M.5
  • 202
  • 205
  • 206
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer G.Z. Glycoprotein folding, quality control and ER-associated degradation. Curr. Opin. Struct. Biol. 2009, 19:515-523.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 207
    • 2342505236 scopus 로고    scopus 로고
    • Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains
    • Frenkel Z., Shenkman M., Kondratyev M., Lederkremer G.Z. Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol. Biol. Cell 2004, 15:2133-2142.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2133-2142
    • Frenkel, Z.1    Shenkman, M.2    Kondratyev, M.3    Lederkremer, G.Z.4
  • 209
    • 67949106610 scopus 로고    scopus 로고
    • Substrate-specific mediators of ER associated degradation (ERAD)
    • Brodsky J.L., Wojcikiewicz R.J. Substrate-specific mediators of ER associated degradation (ERAD). Curr. Opin. Cell Biol. 2009, 21:516-521.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 516-521
    • Brodsky, J.L.1    Wojcikiewicz, R.J.2
  • 211
    • 44649096231 scopus 로고    scopus 로고
    • BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex
    • Wang B., Heath-Engel H., Zhang D., Nguyen N., Thomas D.Y., Hanrahan J.W., Shore G.C. BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex. Cell 2008, 133:1080-1092.
    • (2008) Cell , vol.133 , pp. 1080-1092
    • Wang, B.1    Heath-Engel, H.2    Zhang, D.3    Nguyen, N.4    Thomas, D.Y.5    Hanrahan, J.W.6    Shore, G.C.7
  • 212
    • 48249138088 scopus 로고    scopus 로고
    • Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated degradation
    • Wakana Y., Takai S., Nakajima K., Tani K., Yamamoto A., Watson P., Stephens D.J., Hauri H.P., Tagaya M. Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated degradation. Mol. Biol. Cell 2008, 19:1825-1836.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1825-1836
    • Wakana, Y.1    Takai, S.2    Nakajima, K.3    Tani, K.4    Yamamoto, A.5    Watson, P.6    Stephens, D.J.7    Hauri, H.P.8    Tagaya, M.9
  • 213
    • 77950642050 scopus 로고    scopus 로고
    • The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin
    • Moore P., Bernardi K.M., Tsai B. The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin. Mol. Biol. Cell 2010, 21:1305-1313.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1305-1313
    • Moore, P.1    Bernardi, K.M.2    Tsai, B.3
  • 214
    • 79954423426 scopus 로고    scopus 로고
    • ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER
    • Bernasconi R., Molinari M. ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr. Opin. Cell Biol. 2011, 23(2):176-183.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , Issue.2 , pp. 176-183
    • Bernasconi, R.1    Molinari, M.2
  • 216
    • 0001720417 scopus 로고
    • An address on a characteristic organism of cancer
    • Russell W. An address on a characteristic organism of cancer. Br. Med. J. 1890, 2:1356-1360.
    • (1890) Br. Med. J. , vol.2 , pp. 1356-1360
    • Russell, W.1
  • 217
    • 0344172177 scopus 로고    scopus 로고
    • Multiple myeloma with numerous intranuclear Russell bodies
    • Martin-Noya A., Rios-Herranz E., Rafel-Ribas E. Multiple myeloma with numerous intranuclear Russell bodies. Haematologica 1999, 84:179-180.
    • (1999) Haematologica , vol.84 , pp. 179-180
    • Martin-Noya, A.1    Rios-Herranz, E.2    Rafel-Ribas, E.3
  • 218
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito R.R., Sitia R. Aggresomes and Russell bodies. Symptoms of cellular indigestion?. EMBO Rep. 2000, 1:225-231.
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 219
    • 0026347810 scopus 로고
    • Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum
    • Valetti C., Grossi C.E., Milstein C., Sitia R. Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J. Cell Biol. 1991, 115:983-994.
    • (1991) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Grossi, C.E.2    Milstein, C.3    Sitia, R.4
  • 220
    • 33746032588 scopus 로고    scopus 로고
    • ER storage diseases: a role for ERGIC-53 in controlling the formation and shape of Russell bodies
    • Mattioli L., Anelli T., Fagioli C., Tacchetti C., Sitia R., Valetti C. ER storage diseases: a role for ERGIC-53 in controlling the formation and shape of Russell bodies. J. Cell Sci. 2006, 119:2532-2541.
    • (2006) J. Cell Sci. , vol.119 , pp. 2532-2541
    • Mattioli, L.1    Anelli, T.2    Fagioli, C.3    Tacchetti, C.4    Sitia, R.5    Valetti, C.6
  • 221
    • 77954714045 scopus 로고    scopus 로고
    • Pathogenesis of ER storage disorders: modulating Russell body biogenesis by altering proximal and distal quality control
    • Ronzoni R., Anelli T., Brunati M., Cortini M., Fagioli C., Sitia R. Pathogenesis of ER storage disorders: modulating Russell body biogenesis by altering proximal and distal quality control. Traffic 2010, 11:947-957.
    • (2010) Traffic , vol.11 , pp. 947-957
    • Ronzoni, R.1    Anelli, T.2    Brunati, M.3    Cortini, M.4    Fagioli, C.5    Sitia, R.6
  • 225
    • 27144457472 scopus 로고    scopus 로고
    • Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae
    • Tam Y.Y., Fagarasanu A., Fagarasanu M., Rachubinski R.A. Pex3p initiates the formation of a preperoxisomal compartment from a subdomain of the endoplasmic reticulum in Saccharomyces cerevisiae. J. Biol. Chem. 2005, 280:34933-34939.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34933-34939
    • Tam, Y.Y.1    Fagarasanu, A.2    Fagarasanu, M.3    Rachubinski, R.A.4
  • 226
    • 66749160940 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis
    • Perry R.J., Mast F.D., Rachubinski R.A. Endoplasmic reticulum-associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis. Eukaryot. Cell 2009, 8:830-843.
    • (2009) Eukaryot. Cell , vol.8 , pp. 830-843
    • Perry, R.J.1    Mast, F.D.2    Rachubinski, R.A.3
  • 227
    • 0034717704 scopus 로고    scopus 로고
    • Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis
    • South S.T., Sacksteder K.A., Li X., Liu Y., Gould S.J. Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome synthesis. J. Cell Biol. 2000, 149:1345-1360.
    • (2000) J. Cell Biol. , vol.149 , pp. 1345-1360
    • South, S.T.1    Sacksteder, K.A.2    Li, X.3    Liu, Y.4    Gould, S.J.5
  • 229
    • 33845341438 scopus 로고    scopus 로고
    • Peroxisome biogenesis: where Arf and coatomer might be involved
    • Lay D., Gorgas K., Just W.W. Peroxisome biogenesis: where Arf and coatomer might be involved. Biochim. Biophys. Acta 2006, 1763:1678-1687.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1678-1687
    • Lay, D.1    Gorgas, K.2    Just, W.W.3
  • 231
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B., Waters M.G., Schmitt H.D. Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol. Biol. Cell 2005, 16:3963-3977.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3963-3977
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6    Schmitt, H.D.7
  • 232
    • 0034962022 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- and COPII-mediated vesicular transport
    • Voorn-Brouwer T., Kragt A., Tabak H.F., Distel B. Peroxisomal membrane proteins are properly targeted to peroxisomes in the absence of COPI- and COPII-mediated vesicular transport. J. Cell Sci. 2001, 114:2199-2204.
    • (2001) J. Cell Sci. , vol.114 , pp. 2199-2204
    • Voorn-Brouwer, T.1    Kragt, A.2    Tabak, H.F.3    Distel, B.4
  • 233
  • 234
    • 0014830814 scopus 로고
    • Structure-function relationships in the adipose cell. I. Ultrastructure of the isolated adipose cell
    • Cushman S.W. Structure-function relationships in the adipose cell. I. Ultrastructure of the isolated adipose cell. J. Cell Biol. 1970, 46:326-341.
    • (1970) J. Cell Biol. , vol.46 , pp. 326-341
    • Cushman, S.W.1
  • 235
    • 0033769564 scopus 로고    scopus 로고
    • Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells
    • Wu C.C., Howell K.E., Neville M.C., Yates J.R., McManaman J.L. Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells. Electrophoresis 2000, 21:3470-3482.
    • (2000) Electrophoresis , vol.21 , pp. 3470-3482
    • Wu, C.C.1    Howell, K.E.2    Neville, M.C.3    Yates, J.R.4    McManaman, J.L.5
  • 236
    • 77949524635 scopus 로고    scopus 로고
    • Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets
    • Hodges B.D., Wu C.C. Proteomic insights into an expanded cellular role for cytoplasmic lipid droplets. J. Lipid Res. 2010, 51:262-273.
    • (2010) J. Lipid Res. , vol.51 , pp. 262-273
    • Hodges, B.D.1    Wu, C.C.2
  • 237
    • 54249166513 scopus 로고    scopus 로고
    • Identification and characterization of the ER/lipid droplet-targeting sequence in 17beta-hydroxysteroid dehydrogenase type 11
    • Horiguchi Y., Araki M., Motojima K. Identification and characterization of the ER/lipid droplet-targeting sequence in 17beta-hydroxysteroid dehydrogenase type 11. Arch. Biochem. Biophys. 2008, 479:121-130.
    • (2008) Arch. Biochem. Biophys. , vol.479 , pp. 121-130
    • Horiguchi, Y.1    Araki, M.2    Motojima, K.3
  • 238
    • 46749130169 scopus 로고    scopus 로고
    • Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets
    • Zehmer J.K., Bartz R., Liu P., Anderson R.G. Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets. J. Cell Sci. 2008, 121:1852-1860.
    • (2008) J. Cell Sci. , vol.121 , pp. 1852-1860
    • Zehmer, J.K.1    Bartz, R.2    Liu, P.3    Anderson, R.G.4
  • 239
    • 70350400618 scopus 로고    scopus 로고
    • Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct role in the emergence and regression of lipid droplets
    • Zehmer J.K., Bartz R., Bisel B., Liu P., Seemann J., Anderson R.G. Targeting sequences of UBXD8 and AAM-B reveal that the ER has a direct role in the emergence and regression of lipid droplets. J. Cell Sci. 2009, 122:3694-3702.
    • (2009) J. Cell Sci. , vol.122 , pp. 3694-3702
    • Zehmer, J.K.1    Bartz, R.2    Bisel, B.3    Liu, P.4    Seemann, J.5    Anderson, R.G.6
  • 240
    • 77952954544 scopus 로고    scopus 로고
    • Lipid droplets: a dynamic organelle moves into focus
    • Beller M., Thiel K., Thul P.J., Jackle H. Lipid droplets: a dynamic organelle moves into focus. FEBS Lett. 2010, 584:2176-2182.
    • (2010) FEBS Lett. , vol.584 , pp. 2176-2182
    • Beller, M.1    Thiel, K.2    Thul, P.J.3    Jackle, H.4
  • 241
    • 58149457426 scopus 로고    scopus 로고
    • Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis
    • Yen C.L., Stone S.J., Koliwad S., Harris C., Farese R.V. Thematic review series: glycerolipids. DGAT enzymes and triacylglycerol biosynthesis. J. Lipid Res. 2008, 49:2283-2301.
    • (2008) J. Lipid Res. , vol.49 , pp. 2283-2301
    • Yen, C.L.1    Stone, S.J.2    Koliwad, S.3    Harris, C.4    Farese, R.V.5
  • 242
    • 80051522307 scopus 로고    scopus 로고
    • Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze triacylglycerol synthesis and promote lipid droplet formation independent of its localization to the endoplasmic reticulum
    • (in press).
    • P.J. McFie, S.L. Banman, S. Kary, S.J. Stone, Murine diacylglycerol acyltransferase-2 (DGAT2) can catalyze triacylglycerol synthesis and promote lipid droplet formation independent of its localization to the endoplasmic reticulum, J. Biol. Chem. (in press).
    • J. Biol. Chem.
    • McFie, P.J.1    Banman, S.L.2    Kary, S.3    Stone, S.J.4
  • 243
    • 66349128492 scopus 로고    scopus 로고
    • PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores
    • Bickel P.E., Tansey J.T., Welte M.A. PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim. Biophys. Acta 2009, 1791:419-440.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 419-440
    • Bickel, P.E.1    Tansey, J.T.2    Welte, M.A.3
  • 246
    • 78650107057 scopus 로고    scopus 로고
    • Lipolysis-a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores
    • Lass A., Zimmermann R., Oberer M., Zechner R. Lipolysis-a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores. Prog. Lipid Res. 2011, 50:14-27.
    • (2011) Prog. Lipid Res. , vol.50 , pp. 14-27
    • Lass, A.1    Zimmermann, R.2    Oberer, M.3    Zechner, R.4
  • 247
    • 0037018773 scopus 로고    scopus 로고
    • Endoplasmic reticulum storage diseases
    • Rutishauser J., Spiess M. Endoplasmic reticulum storage diseases. Swiss Med. Wkly. 2002, 132:211-222.
    • (2002) Swiss Med. Wkly. , vol.132 , pp. 211-222
    • Rutishauser, J.1    Spiess, M.2
  • 248
    • 35748931161 scopus 로고    scopus 로고
    • Raft-dependent endocytosis of autocrine motility factor is phosphatidylinositol 3-kinase-dependent in breast carcinoma cells
    • Kojic L.D., Joshi B., Lajoie P., Le P.U., Cox M.E., Turbin D.A., Wiseman S.M., Nabi I.R. Raft-dependent endocytosis of autocrine motility factor is phosphatidylinositol 3-kinase-dependent in breast carcinoma cells. J. Biol. Chem. 2007, 282:29305-29313.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29305-29313
    • Kojic, L.D.1    Joshi, B.2    Lajoie, P.3    Le, P.U.4    Cox, M.E.5    Turbin, D.A.6    Wiseman, S.M.7    Nabi, I.R.8
  • 250
    • 77950556316 scopus 로고    scopus 로고
    • A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase
    • Joshi B., Li L., Nabi I.R. A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase. J. Biol. Chem. 2010, 285:8830-8839.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8830-8839
    • Joshi, B.1    Li, L.2    Nabi, I.R.3
  • 251
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 2002, 16:1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 252
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 253
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding H.P., Zhang Y., Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999, 397:271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 254
    • 0032920099 scopus 로고    scopus 로고
    • Amino acid limitation regulates CHOP expression through a specific pathway independent of the unfolded protein response
    • Jousse C., Bruhat A., Harding H.P., Ferrara M., Ron D., Fafournoux P. Amino acid limitation regulates CHOP expression through a specific pathway independent of the unfolded protein response. FEBS Lett. 1999, 448:211-216.
    • (1999) FEBS Lett. , vol.448 , pp. 211-216
    • Jousse, C.1    Bruhat, A.2    Harding, H.P.3    Ferrara, M.4    Ron, D.5    Fafournoux, P.6
  • 257
    • 79959897450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and pancreatic beta-cell death
    • Fonseca S.G., Gromada J., Urano F. Endoplasmic reticulum stress and pancreatic beta-cell death. Trends Endocrinol. Metab. 2011, 22(7):266-274.
    • (2011) Trends Endocrinol. Metab. , vol.22 , Issue.7 , pp. 266-274
    • Fonseca, S.G.1    Gromada, J.2    Urano, F.3
  • 258
    • 33646166752 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis and auto-immunity in diabetes
    • Lipson K.L., Fonseca S.G., Urano F. Endoplasmic reticulum stress-induced apoptosis and auto-immunity in diabetes. Curr. Mol. Med. 2006, 6:71-77.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 71-77
    • Lipson, K.L.1    Fonseca, S.G.2    Urano, F.3
  • 259
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito O.M., Scorrano L. An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J. 2010, 29:2715-2723.
    • (2010) EMBO J. , vol.29 , pp. 2715-2723
    • de Brito, O.M.1    Scorrano, L.2
  • 262
    • 80051802321 scopus 로고    scopus 로고
    • The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites, Cell Death Differ
    • (in press).
    • P. Pinton, C. Giorgi, P.P. Pandolfi, The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites, Cell Death Differ. (in press).
    • Pinton, P.1    Giorgi, C.2    Pandolfi, P.P.3
  • 265
    • 40149104688 scopus 로고    scopus 로고
    • Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells
    • Bozidis P., Williamson C.D., Colberg-Poley A.M. Mitochondrial and secretory human cytomegalovirus UL37 proteins traffic into mitochondrion-associated membranes of human cells. J. Virol. 2008, 82:2715-2726.
    • (2008) J. Virol. , vol.82 , pp. 2715-2726
    • Bozidis, P.1    Williamson, C.D.2    Colberg-Poley, A.M.3
  • 266
    • 79551703425 scopus 로고    scopus 로고
    • The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts
    • Williamson C.D., Zhang A., Colberg-Poley A.M. The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts. J. Virol. 2011, 85:2100-2111.
    • (2011) J. Virol. , vol.85 , pp. 2100-2111
    • Williamson, C.D.1    Zhang, A.2    Colberg-Poley, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.