메뉴 건너뛰기




Volumn 18, Issue 4, 2006, Pages 371-378

Inter-organelle membrane contact sites: through a glass, darkly

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LIPID TRANSFER PROTEIN; MEMBRANE PROTEIN; OXYSTEROL; PHOSPHOLIPID DERIVATIVE; STEROL;

EID: 33745755614     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2006.06.011     Document Type: Review
Times cited : (195)

References (76)
  • 1
    • 20444410101 scopus 로고    scopus 로고
    • Presynaptic calcium stores and synaptic transmission
    • Collin T., Marty A., and Llano I. Presynaptic calcium stores and synaptic transmission. Curr Opin Neurobiol 15 (2005) 275-281
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 275-281
    • Collin, T.1    Marty, A.2    Llano, I.3
  • 2
    • 0141754206 scopus 로고    scopus 로고
    • Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria
    • Filippin L., Magalhaes P.J., Di Benedetto G., Colella M., and Pozzan T. Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria. J Biol Chem 278 (2003) 39224-39234
    • (2003) J Biol Chem , vol.278 , pp. 39224-39234
    • Filippin, L.1    Magalhaes, P.J.2    Di Benedetto, G.3    Colella, M.4    Pozzan, T.5
  • 3
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • Vance J.E. Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism. Prog Nucleic Acid Res Mol Biol 75 (2003) 69-111
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 4
    • 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., and 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 268 (2001) 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
  • 5
    • 0033944449 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p
    • Pan X., Roberts P., Chen Y., Kvam E., Shulga N., Huang K., Lemmon S., and Goldfarb D.S. Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p. Mol Biol Cell 11 (2000) 2445-2457
    • (2000) Mol Biol Cell , vol.11 , pp. 2445-2457
    • Pan, X.1    Roberts, P.2    Chen, Y.3    Kvam, E.4    Shulga, N.5    Huang, K.6    Lemmon, S.7    Goldfarb, D.S.8
  • 6
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • Urbani L., and Simoni R.D. Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane. J Biol Chem 265 (1990) 1919-1923
    • (1990) J Biol Chem , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 7
    • 0033565535 scopus 로고    scopus 로고
    • Resynthesis of phosphatidylinositol in permeabilized neutrophils following phospholipase Cβ activation: transport of the intermediate, phosphatidic acid, from the plasma membrane to the endoplasmic reticulum for phosphatidylinositol resynthesis is not dependent on soluble lipid carriers or vesicular transport
    • Whatmore J., Wiedemann C., Somerharju P., Swigart P., and Cockcroft S. Resynthesis of phosphatidylinositol in permeabilized neutrophils following phospholipase Cβ activation: transport of the intermediate, phosphatidic acid, from the plasma membrane to the endoplasmic reticulum for phosphatidylinositol resynthesis is not dependent on soluble lipid carriers or vesicular transport. Biochem J 341 (1999) 435-444
    • (1999) Biochem J , vol.341 , pp. 435-444
    • Whatmore, J.1    Wiedemann, C.2    Somerharju, P.3    Swigart, P.4    Cockcroft, S.5
  • 8
    • 0029842873 scopus 로고    scopus 로고
    • Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle
    • Flucher B.E., and Franzini-Armstrong C. Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle. Proc Natl Acad Sci U S A 93 (1996) 8101-8106
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8101-8106
    • Flucher, B.E.1    Franzini-Armstrong, C.2
  • 9
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • Loewen C.J., Roy A., and Levine T.P. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J 22 (2003) 2025-2035
    • (2003) EMBO J , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 10
    • 0442292211 scopus 로고    scopus 로고
    • The exocyst meets the translocon: a regulatory circuit for secretion and protein synthesis?
    • Guo W., and Novick P. The exocyst meets the translocon: a regulatory circuit for secretion and protein synthesis?. Trends Cell Biol 14 (2004) 61-63
    • (2004) Trends Cell Biol , vol.14 , pp. 61-63
    • Guo, W.1    Novick, P.2
  • 11
    • 0033636778 scopus 로고    scopus 로고
    • Junctophilins: a novel family of junctional membrane complex proteins
    • Takeshima H., Komazaki S., Nishi M., Iino M., and Kangawa K. Junctophilins: a novel family of junctional membrane complex proteins. Mol Cell 6 (2000) 11-22
    • (2000) Mol Cell , vol.6 , pp. 11-22
    • Takeshima, H.1    Komazaki, S.2    Nishi, M.3    Iino, M.4    Kangawa, K.5
  • 12
    • 15244340169 scopus 로고    scopus 로고
    • Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages
    • Becker T., Volchuk A., and Rothman J.E. Differential use of endoplasmic reticulum membrane for phagocytosis in J774 macrophages. Proc Natl Acad Sci U S A 102 (2005) 4022-4026
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4022-4026
    • Becker, T.1    Volchuk, A.2    Rothman, J.E.3
  • 14
    • 1842589369 scopus 로고    scopus 로고
    • A novel transport pathway for a yeast plasma membrane protein encoded by a localized mRNA
    • Juschke C., Ferring D., Jansen R.P., and Seedorf M. A novel transport pathway for a yeast plasma membrane protein encoded by a localized mRNA. Curr Biol 14 (2004) 406-411
    • (2004) Curr Biol , vol.14 , pp. 406-411
    • Juschke, C.1    Ferring, D.2    Jansen, R.P.3    Seedorf, M.4
  • 15
    • 22044445588 scopus 로고    scopus 로고
    • SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane
    • Juschke C., Wachter A., Schwappach B., and Seedorf M. SEC18/NSF-independent, protein-sorting pathway from the yeast cortical ER to the plasma membrane. J Cell Biol 169 (2005) 613-622
    • (2005) J Cell Biol , vol.169 , pp. 613-622
    • Juschke, C.1    Wachter, A.2    Schwappach, B.3    Seedorf, M.4
  • 16
    • 18144409111 scopus 로고    scopus 로고
    • 2+ release triggers translocation of membrane marker FM1-43 from the extracellular leaflet of the plasma membrane into endoplasmic reticulum in T lymphocytes
    • 2+ release triggers translocation of membrane marker FM1-43 from the extracellular leaflet of the plasma membrane into endoplasmic reticulum in T lymphocytes. J Biol Chem 280 (2005) 16377-16382
    • (2005) J Biol Chem , vol.280 , pp. 16377-16382
    • Dadsetan, S.1    Shishkin, V.2    Fomina, A.F.3
  • 17
    • 4344664038 scopus 로고    scopus 로고
    • Dynamics and inheritance of the endoplasmic reticulum
    • Du Y., Ferro-Novick S., and Novick P. Dynamics and inheritance of the endoplasmic reticulum. J Cell Sci 117 (2004) 2871-2878
    • (2004) J Cell Sci , vol.117 , pp. 2871-2878
    • Du, Y.1    Ferro-Novick, S.2    Novick, P.3
  • 18
    • 14044255694 scopus 로고    scopus 로고
    • Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae
    • Estrada de Martin P., Du Y., Novick P., and Ferro-Novick S. Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae. J Cell Sci 118 (2005) 65-77
    • (2005) J Cell Sci , vol.118 , pp. 65-77
    • Estrada de Martin, P.1    Du, Y.2    Novick, P.3    Ferro-Novick, S.4
  • 19
    • 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., and Rapoport T.A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124 (2006) 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
  • 21
    • 0038461879 scopus 로고    scopus 로고
    • Macrophage cholesterol transport: a critical player in foam cell formation
    • Vainio S., and Ikonen E. Macrophage cholesterol transport: a critical player in foam cell formation. Ann Med 35 (2003) 146-155
    • (2003) Ann Med , vol.35 , pp. 146-155
    • Vainio, S.1    Ikonen, E.2
  • 22
    • 17444368686 scopus 로고    scopus 로고
    • Direct observation of rapid internalization and intracellular transport of sterol by macrophage foam cells
    • Wustner D., Mondal M., Tabas I., and Maxfield F.R. Direct observation of rapid internalization and intracellular transport of sterol by macrophage foam cells. Traffic 6 (2005) 396-412
    • (2005) Traffic , vol.6 , pp. 396-412
    • Wustner, D.1    Mondal, M.2    Tabas, I.3    Maxfield, F.R.4
  • 23
    • 7244238074 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transporters mediate nonvesicular, raft-modulated sterol movement from the plasma membrane to the endoplasmic reticulum
    • The Prinz lab show that transport of sterol from the PM to the ER in yeast requires two ATP-binding cassette (ABC)-transporters in the PM, and that traffic is non-vesicular (independent of NSF/Sec18). This retrograde traffic is inversely correlated with the ability of sterols to form complexes with sphingolipids in the PM.
    • Li Y., and 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 279 (2004) 45226-45234. The Prinz lab show that transport of sterol from the PM to the ER in yeast requires two ATP-binding cassette (ABC)-transporters in the PM, and that traffic is non-vesicular (independent of NSF/Sec18). This retrograde traffic is inversely correlated with the ability of sterols to form complexes with sphingolipids in the PM.
    • (2004) J Biol Chem , vol.279 , pp. 45226-45234
    • Li, Y.1    Prinz, W.A.2
  • 24
    • 17144403817 scopus 로고    scopus 로고
    • Transport of newly synthesized sterol to the sterol-enriched plasma membrane occurs via non-vesicular equilibration
    • Menon and colleagues use a sterol export assay to demonstrate highly efficient non-vesicular traffic of ergosterol in yeast, independent of NSF/Sec18. This confirms older observations by Simoni and co-workers in mammalian cells [6], and allows further genetic experiments, showing that sphingolipid (presumably in the plasma membrane) acts as a sink for free sterol, allowing a high total sterol to build up.
    • Baumann N., Sullivan D., Ohvo-Rekilä H., Simonot C., Pottekat A., Klaassen Z., Beh C., and Menon A. Transport of newly synthesized sterol to the sterol-enriched plasma membrane occurs via non-vesicular equilibration. Biochemistry 44 (2005) 5816-5826. Menon and colleagues use a sterol export assay to demonstrate highly efficient non-vesicular traffic of ergosterol in yeast, independent of NSF/Sec18. This confirms older observations by Simoni and co-workers in mammalian cells [6], and allows further genetic experiments, showing that sphingolipid (presumably in the plasma membrane) acts as a sink for free sterol, allowing a high total sterol to build up.
    • (2005) Biochemistry , vol.44 , pp. 5816-5826
    • Baumann, N.1    Sullivan, D.2    Ohvo-Rekilä, H.3    Simonot, C.4    Pottekat, A.5    Klaassen, Z.6    Beh, C.7    Menon, A.8
  • 27
    • 0019168614 scopus 로고
    • Cytosolic proteins that bind oxygenated sterols. Cellular distribution, specificity, and some properties
    • Kandutsch A.A., and Thompson E.B. Cytosolic proteins that bind oxygenated sterols. Cellular distribution, specificity, and some properties. J Biol Chem 255 (1980) 10813-10821
    • (1980) J Biol Chem , vol.255 , pp. 10813-10821
    • Kandutsch, A.A.1    Thompson, E.B.2
  • 29
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Hurley and colleagues solve the structure of an oxysterol binding protein, showing that they all share a hydrophobic pocket that accommodates a single sterol (with little specificity for any particular [oxy-]sterol), suggesting that they are all capable of acting as sterol transfer proteins, and pointing to a transfer mechanism, whereby the lid above the pocket binds to anionic phospholipids before opening to allow sterol exchange.
    • Im Y.J., Raychaudhuri S., Prinz W.A., and Hurley J.H. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437 (2005) 154-158. Hurley and colleagues solve the structure of an oxysterol binding protein, showing that they all share a hydrophobic pocket that accommodates a single sterol (with little specificity for any particular [oxy-]sterol), suggesting that they are all capable of acting as sterol transfer proteins, and pointing to a transfer mechanism, whereby the lid above the pocket binds to anionic phospholipids before opening to allow sterol exchange.
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 30
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • ••] to show that yeast OSBP homologues transfer sterols in vivo (Osh3 and Osh5 being the most likely candidates) and in vitro. Also, a detailed study of one homologue (Osh4/Kes1) confirms predictions that this lipid traffic by OSBP homologues is stimulated by interactions with phosphoinositides, presumably in both donor and acceptor membranes.
    • ••] to show that yeast OSBP homologues transfer sterols in vivo (Osh3 and Osh5 being the most likely candidates) and in vitro. Also, a detailed study of one homologue (Osh4/Kes1) confirms predictions that this lipid traffic by OSBP homologues is stimulated by interactions with phosphoinositides, presumably in both donor and acceptor membranes.
    • (2006) J Cell Biol , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 31
    • 33745475883 scopus 로고    scopus 로고
    • Sterol traffi{ligature}cking between the endoplasmic reticulum and plasma membrane in yeast
    • Sullivan D.P., Ohvo-Rekilä H., Baumann N.A., Beh C.T., and Menon A.K. Sterol traffi{ligature}cking between the endoplasmic reticulum and plasma membrane in yeast. Biochem Soc Trans 34 (2006) 356-358
    • (2006) Biochem Soc Trans , vol.34 , pp. 356-358
    • Sullivan, D.P.1    Ohvo-Rekilä, H.2    Baumann, N.A.3    Beh, C.T.4    Menon, A.K.5
  • 32
    • 2642558199 scopus 로고    scopus 로고
    • Oxysterol binding protein and its homologues: new regulatory factors involved in lipid metabolism
    • Olkkonen V.M. Oxysterol binding protein and its homologues: new regulatory factors involved in lipid metabolism. Curr Opin Lipidol 15 (2004) 321-327
    • (2004) Curr Opin Lipidol , vol.15 , pp. 321-327
    • Olkkonen, V.M.1
  • 34
    • 26844518949 scopus 로고    scopus 로고
    • Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants
    • Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvarinen K., and Olkkonen V.M. Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants. Exp Cell Res 310 (2005) 445-462
    • (2005) Exp Cell Res , vol.310 , pp. 445-462
    • Lehto, M.1    Hynynen, R.2    Karjalainen, K.3    Kuismanen, E.4    Hyvarinen, K.5    Olkkonen, V.M.6
  • 35
    • 2342447668 scopus 로고    scopus 로고
    • Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7
    • Lehto M., Tienari J., Lehtonen S., Lehtonen E., and Olkkonen V.M. Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7. Cell Tissue Res 315 (2004) 39-57
    • (2004) Cell Tissue Res , vol.315 , pp. 39-57
    • Lehto, M.1    Tienari, J.2    Lehtonen, S.3    Lehtonen, E.4    Olkkonen, V.M.5
  • 36
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol 14 (2004) 483-490
    • (2004) Trends Cell Biol , vol.14 , pp. 483-490
    • Levine, T.1
  • 37
    • 25444529050 scopus 로고    scopus 로고
    • AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism
    • Wang P., Zhang Y., Li H., Chieu H.K., Munn A.L., and Yang H. AAA ATPases regulate membrane association of yeast oxysterol binding proteins and sterol metabolism. EMBO J 24 (2005) 2989-2999
    • (2005) EMBO J , vol.24 , pp. 2989-2999
    • Wang, P.1    Zhang, Y.2    Li, H.3    Chieu, H.K.4    Munn, A.L.5    Yang, H.6
  • 38
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and VAMP-associated protein are required for sterol-dependent activation of the ceramide transport protein
    • Perry and Ridgway provide a molecular explanation for a previous finding that oxysterols stimulate sphingolipid production. They show that when changes in sterol metabolism induce the translocation of OSBP to the TGN, the ceramide transporter (CERT) also translocates to Golgi membranes, transporting more ceramide to sphingomyelin synthase at that site, as predicted by Hanada [49].
    • Perry R.J., and Ridgway N.D. Oxysterol-binding protein and VAMP-associated protein are required for sterol-dependent activation of the ceramide transport protein. Mol Biol Cell 17 (2006) 2604-2616. Perry and Ridgway provide a molecular explanation for a previous finding that oxysterols stimulate sphingolipid production. They show that when changes in sterol metabolism induce the translocation of OSBP to the TGN, the ceramide transporter (CERT) also translocates to Golgi membranes, transporting more ceramide to sphingomyelin synthase at that site, as predicted by Hanada [49].
    • (2006) Mol Biol Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 40
    • 14744294236 scopus 로고    scopus 로고
    • Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
    • Litvak V., Dahan N., Ramachandran S., Sabanay H., and Lev S. Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat Cell Biol 7 (2005) 225-234
    • (2005) Nat Cell Biol , vol.7 , pp. 225-234
    • Litvak, V.1    Dahan, N.2    Ramachandran, S.3    Sabanay, H.4    Lev, S.5
  • 41
    • 27744604253 scopus 로고    scopus 로고
    • Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast
    • Routt S.M., Ryan M.M., Tyeryar K., Rizzieri K.E., Mousley C., Roumanie O., Brennwald P.J., and Bankaitis V.A. Nonclassical PITPs activate PLD via the Stt4p PtdIns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast. Traffic 6 (2005) 1157-1172
    • (2005) Traffic , vol.6 , pp. 1157-1172
    • Routt, S.M.1    Ryan, M.M.2    Tyeryar, K.3    Rizzieri, K.E.4    Mousley, C.5    Roumanie, O.6    Brennwald, P.J.7    Bankaitis, V.A.8
  • 43
    • 0027216545 scopus 로고
    • Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein
    • Vihtelic T.S., Goebl M., Milligan S., O'Tousa J.E., and Hyde D.R. Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein. J Cell Biol 122 (1993) 1013-1022
    • (1993) J Cell Biol , vol.122 , pp. 1013-1022
    • Vihtelic, T.S.1    Goebl, M.2    Milligan, S.3    O'Tousa, J.E.4    Hyde, D.R.5
  • 44
    • 0034635374 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein
    • Goldstein B.J., Bittner-Kowalczyk A., White M.F., and Harbeck M. Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein. J Biol Chem 275 (2000) 4283-4289
    • (2000) J Biol Chem , vol.275 , pp. 4283-4289
    • Goldstein, B.J.1    Bittner-Kowalczyk, A.2    White, M.F.3    Harbeck, M.4
  • 45
    • 33646800165 scopus 로고    scopus 로고
    • ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
    • Arregui and co-workers co-localise Src and FAK in focal adhesions with a substrate-trapping mutant of PTP-1B on the ER in the puncta that form at the tips of ER tubules that are pulled out of the central ER network on microtubules.
    • Hernandez M.V., Sala M.G., Balsamo J., Lilien J., and Arregui C.O. ER-bound PTP1B is targeted to newly forming cell-matrix adhesions. J Cell Sci 119 (2006) 1233-1243. Arregui and co-workers co-localise Src and FAK in focal adhesions with a substrate-trapping mutant of PTP-1B on the ER in the puncta that form at the tips of ER tubules that are pulled out of the central ER network on microtubules.
    • (2006) J Cell Sci , vol.119 , pp. 1233-1243
    • Hernandez, M.V.1    Sala, M.G.2    Balsamo, J.3    Lilien, J.4    Arregui, C.O.5
  • 47
    • 30344474272 scopus 로고    scopus 로고
    • 2+ signaling microdomains: platforms for the assembly and regulation of TRPC channels
    • 2+ signaling microdomains: platforms for the assembly and regulation of TRPC channels. Trends Pharmacol Sci 27 (2006) 25-32
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 25-32
    • Ambudkar, I.S.1
  • 48
    • 2442640305 scopus 로고    scopus 로고
    • Predicting function from structure: 3D structure studies of the mammalian Golgi complex
    • Mogelsvang S., Marsh B.J., Ladinsky M.S., and Howell K.E. Predicting function from structure: 3D structure studies of the mammalian Golgi complex. Traffic 5 (2004) 338-345
    • (2004) Traffic , vol.5 , pp. 338-345
    • Mogelsvang, S.1    Marsh, B.J.2    Ladinsky, M.S.3    Howell, K.E.4
  • 49
    • 33646227441 scopus 로고    scopus 로고
    • Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide
    • Hanada K. Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide. Mol Cell Biochem (2006)
    • (2006) Mol Cell Biochem
    • Hanada, K.1
  • 50
    • 2342597726 scopus 로고    scopus 로고
    • Genetic analysis of intracellular aminoglycerophospholipid traffic
    • Voelker D.R. Genetic analysis of intracellular aminoglycerophospholipid traffic. Biochem Cell Biol 82 (2004) 156-169
    • (2004) Biochem Cell Biol , vol.82 , pp. 156-169
    • Voelker, D.R.1
  • 51
    • 1342346595 scopus 로고    scopus 로고
    • Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process
    • This dissection of phosphatidylserine (PS) traffic in a model system by the Voelker lab shows that Golgi acceptor vesicles need to include both the PS utilising enzyme, which contains a critical C2 domain that binds the headgroups of lipids on donor vesicles, and Sfh4. Among the artificial PS donors used, only those with very high concentrations of PS and phosphatidic acid were active, setting the scene for the next step in which physiological donors are used and the entire inter-organelle lipid traffic machinery is reconstituted.
    • Wu W.I., and Voelker D.R. Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process. J Biol Chem 279 (2004) 6635-6642. This dissection of phosphatidylserine (PS) traffic in a model system by the Voelker lab shows that Golgi acceptor vesicles need to include both the PS utilising enzyme, which contains a critical C2 domain that binds the headgroups of lipids on donor vesicles, and Sfh4. Among the artificial PS donors used, only those with very high concentrations of PS and phosphatidic acid were active, setting the scene for the next step in which physiological donors are used and the entire inter-organelle lipid traffic machinery is reconstituted.
    • (2004) J Biol Chem , vol.279 , pp. 6635-6642
    • Wu, W.I.1    Voelker, D.R.2
  • 52
    • 14044268935 scopus 로고    scopus 로고
    • Differential regulation of ER structure through VAP-Nir protein interaction
    • Amarilio R., Ramachandran S., Sabanay H., and Lev S. Differential regulation of ER structure through VAP-Nir protein interaction. J Biol Chem 280 (2005) 5933-5944
    • (2005) J Biol Chem , vol.280 , pp. 5933-5944
    • Amarilio, R.1    Ramachandran, S.2    Sabanay, H.3    Lev, S.4
  • 53
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine T.P., and Munro S. Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol Biol Cell 12 (2001) 1633-1644
    • (2001) Mol Biol Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 54
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • Kvam E., and Goldfarb D.S. Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae. J Cell Sci 117 (2004) 4959-4968
    • (2004) J Cell Sci , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 55
    • 24344449583 scopus 로고    scopus 로고
    • Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles
    • Kvam E., Gable K., Dunn T.M., and Goldfarb D.S. Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol Biol Cell 16 (2005) 3987-3998
    • (2005) Mol Biol Cell , vol.16 , pp. 3987-3998
    • Kvam, E.1    Gable, K.2    Dunn, T.M.3    Goldfarb, D.S.4
  • 56
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson M., Lehto M., Tanhuanpaa K., Cover T.L., and Olkkonen V.M. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell 16 (2005) 5480-5492
    • (2005) Mol Biol Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 57
    • 0035163949 scopus 로고    scopus 로고
    • Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events
    • Ko D.C., Gordon M.D., Jin J.Y., and Scott M.P. Dynamic movements of organelles containing Niemann-Pick C1 protein: NPC1 involvement in late endocytic events. Mol Biol Cell 12 (2001) 601-614
    • (2001) Mol Biol Cell , vol.12 , pp. 601-614
    • Ko, D.C.1    Gordon, M.D.2    Jin, J.Y.3    Scott, M.P.4
  • 58
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj F.G., Verveer P.J., Squire A., Neel B.G., and Bastiaens P.I. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295 (2002) 1708-1711
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 59
    • 33646004283 scopus 로고    scopus 로고
    • Mutation of the TGD1 chloroplast envelope protein affects phosphatidate metabolism in Arabidopsis
    • Xu C., Fan J., Froehlich J.E., Awai K., and Benning C. Mutation of the TGD1 chloroplast envelope protein affects phosphatidate metabolism in Arabidopsis. Plant Cell 17 (2005) 3094-3110
    • (2005) Plant Cell , vol.17 , pp. 3094-3110
    • Xu, C.1    Fan, J.2    Froehlich, J.E.3    Awai, K.4    Benning, C.5
  • 60
    • 0028916511 scopus 로고
    • Characterization of a microsomal subfraction associated with mitochondria of the yeast. Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria
    • Gaigg B., Simbeni R., Hrastnik C., Paltauf F., and Daum G. Characterization of a microsomal subfraction associated with mitochondria of the yeast. Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria. Biochim Biophys Acta 1234 (1995) 214-220
    • (1995) Biochim Biophys Acta , vol.1234 , pp. 214-220
    • Gaigg, B.1    Simbeni, R.2    Hrastnik, C.3    Paltauf, F.4    Daum, G.5
  • 62
    • 20144385980 scopus 로고    scopus 로고
    • PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis
    • Thomas and co-workers have found that PACS-2 regulates mitochondrial-ER cross-talk, as when PACS-2 is knocked-down, mitochondria fragment and the amount of MAM decreases. The importance of information traffic between the ER and mitochondria is stressed by the finding that upon induction of apoptosis PACS-2 translocates from ER to mitochondria, where it induces apoptosis by recruiting Bid.
    • Simmen T., Aslan J.E., Blagoveshchenskaya A.D., Thomas L., Wan L., Xiang Y., Feliciangeli S.F., Hung C.H., Crump C.M., and Thomas G. PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis. EMBO J 24 (2005) 717-729. Thomas and co-workers have found that PACS-2 regulates mitochondrial-ER cross-talk, as when PACS-2 is knocked-down, mitochondria fragment and the amount of MAM decreases. The importance of information traffic between the ER and mitochondria is stressed by the finding that upon induction of apoptosis PACS-2 translocates from ER to mitochondria, where it induces apoptosis by recruiting Bid.
    • (2005) EMBO J , vol.24 , pp. 717-729
    • Simmen, T.1    Aslan, J.E.2    Blagoveshchenskaya, A.D.3    Thomas, L.4    Wan, L.5    Xiang, Y.6    Feliciangeli, S.F.7    Hung, C.H.8    Crump, C.M.9    Thomas, G.10
  • 63
    • 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., and Nabi I.R. Calcium regulates the association between mitochondria and a smooth subdomain of the endoplasmic reticulum. J Cell Biol 150 (2000) 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
  • 64
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk H.A., and Yaffe M.P. A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J Cell Biol 145 (1999) 1199-1208
    • (1999) J Cell Biol , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 65
    • 0037185026 scopus 로고    scopus 로고
    • Phosphatidylserine transport to the mitochondria is regulated by ubiquitination
    • Schumacher M.M., Choi J.Y., and Voelker D.R. Phosphatidylserine transport to the mitochondria is regulated by ubiquitination. J Biol Chem 277 (2002) 51033-51042
    • (2002) J Biol Chem , vol.277 , pp. 51033-51042
    • Schumacher, M.M.1    Choi, J.Y.2    Voelker, D.R.3
  • 66
    • 0037009088 scopus 로고    scopus 로고
    • Contact sites between the outer and inner membrane of mitochondria-role in protein transport
    • Reichert A.S., and Neupert W. Contact sites between the outer and inner membrane of mitochondria-role in protein transport. Biochim Biophys Acta 1592 (2002) 41-49
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 41-49
    • Reichert, A.S.1    Neupert, W.2
  • 67
    • 20244373481 scopus 로고    scopus 로고
    • Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17
    • Work from the Pfanner lab showing that Tim21 in the IMM links the TIM23 complex to Tom22 in the TOM complex, and that two forms of TIM23 complex can be defined by the presence/absence of Tim21, switching from a state that captures polypeptide from TOM, to a state that passes incoming proteins to the matrix.
    • Chacinska A., Lind M., Frazier A.E., Dudek J., Meisinger C., Geissler A., Sickmann A., Meyer H.E., Truscott K.N., Guiard B., et al. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120 (2005) 817-829. Work from the Pfanner lab showing that Tim21 in the IMM links the TIM23 complex to Tom22 in the TOM complex, and that two forms of TIM23 complex can be defined by the presence/absence of Tim21, switching from a state that captures polypeptide from TOM, to a state that passes incoming proteins to the matrix.
    • (2005) Cell , vol.120 , pp. 817-829
    • Chacinska, A.1    Lind, M.2    Frazier, A.E.3    Dudek, J.4    Meisinger, C.5    Geissler, A.6    Sickmann, A.7    Meyer, H.E.8    Truscott, K.N.9    Guiard, B.10
  • 68
    • 21244458136 scopus 로고    scopus 로고
    • Role of Tim21 in mitochondrial translocation contact sites
    • Mokranjac D., Popov-Celeketic D., Hell K., and Neupert W. Role of Tim21 in mitochondrial translocation contact sites. J Biol Chem 280 (2005) 23437-23440
    • (2005) J Biol Chem , vol.280 , pp. 23437-23440
    • Mokranjac, D.1    Popov-Celeketic, D.2    Hell, K.3    Neupert, W.4
  • 70
    • 0142105410 scopus 로고    scopus 로고
    • Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    • Chacinska A., Rehling P., Guiard B., Frazier A.E., Schulze-Specking A., Pfanner N., Voos W., and Meisinger C. Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J 22 (2003) 5370-5381
    • (2003) EMBO J , vol.22 , pp. 5370-5381
    • Chacinska, A.1    Rehling, P.2    Guiard, B.3    Frazier, A.E.4    Schulze-Specking, A.5    Pfanner, N.6    Voos, W.7    Meisinger, C.8
  • 71
    • 12844260125 scopus 로고    scopus 로고
    • Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane
    • •] may modulate general OMM-IMM inter-relatedness, they are not the glue that holds the two membranes together.
    • •] may modulate general OMM-IMM inter-relatedness, they are not the glue that holds the two membranes together.
    • (2005) Biochem J , vol.385 , pp. 445-450
    • Speer, O.1    Back, N.2    Buerklen, T.3    Brdiczka, D.4    Koretsky, A.5    Wallimann, T.6    Eriksson, O.7
  • 72
    • 0030787527 scopus 로고    scopus 로고
    • In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate
    • Schulke N., Sepuri N.B., and Pain D. In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate. Proc Natl Acad Sci U S A 94 (1997) 7314-7319
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 7314-7319
    • Schulke, N.1    Sepuri, N.B.2    Pain, D.3
  • 73
    • 0038586417 scopus 로고    scopus 로고
    • Continuous equilibration of phosphatidylcholine and its precursors between endoplasmic reticulum and mitochondria in yeast
    • de Kroon A.I., Koorengevel M.C., Vromans T.A., and de Kruijff B. Continuous equilibration of phosphatidylcholine and its precursors between endoplasmic reticulum and mitochondria in yeast. Mol Biol Cell 14 (2003) 2142-2150
    • (2003) Mol Biol Cell , vol.14 , pp. 2142-2150
    • de Kroon, A.I.1    Koorengevel, M.C.2    Vromans, T.A.3    de Kruijff, B.4
  • 74
    • 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., and Daum G. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur J Biochem 264 (1999) 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
  • 75
    • 0032055479 scopus 로고    scopus 로고
    • A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria
    • Shiao Y.J., Balcerzak B., and Vance J.E. A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria. Biochem J 331 (1998) 217-223
    • (1998) Biochem J , vol.331 , pp. 217-223
    • Shiao, Y.J.1    Balcerzak, B.2    Vance, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.