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Volumn 116, Issue 23, 2003, Pages 4821-4832

The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics

Author keywords

Cholesterol; Endosomes; Golgi; p24 proteins; Raft; Structure

Indexed keywords

CHOLESTEROL; GAG PROTEIN; LIPID; MEMBRANE PROTEIN; MUTANT PROTEIN; OLIGOMER; PROTEIN P25; TRANSFERRIN RECEPTOR;

EID: 0347382331     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00802     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 0033523767 scopus 로고    scopus 로고
    • Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin
    • Abrami, L. and van der Goot, F. G. (1999). Plasma membrane microdomains act as concentration platforms to facilitate intoxication by aerolysin. J. Cell Biol. 147, 175-184.
    • (1999) J. Cell Biol. , vol.147 , pp. 175-184
    • Abrami, L.1    van der Goot, F.G.2
  • 2
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • Barr, F. A., Preisinger, C., Kopajtich, R. and Korner, R. (2001). Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J. Cell Biol. 155, 885-891.
    • (2001) J. Cell Biol. , vol.155 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Korner, R.4
  • 3
    • 0035159694 scopus 로고    scopus 로고
    • Deletion of Yeast p24 Genes Activates the Unfolded Protein Response
    • Belden, W. J. and Barlowe, C. (2001). Deletion of Yeast p24 Genes Activates the Unfolded Protein Response. Mol. Biol. Cell 12, 957-969.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 957-969
    • Belden, W.J.1    Barlowe, C.2
  • 6
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C. and Okayama, H. (1987). High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell Biol. 7, 2745-2752.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 7
    • 0034708445 scopus 로고    scopus 로고
    • Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway
    • Ciufo, L. F. and Boyd, A. (2000). Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway. J. Biol. Chem. 275, 8382-8388.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8382-8388
    • Ciufo, L.F.1    Boyd, A.2
  • 10
    • 0033577863 scopus 로고    scopus 로고
    • Fusogenic domains of golgi membranes are sequestered into specialized regions of the stack that can be released by mechanical fragmentation
    • Dominguez, M., Fazel, A., Dahan, S., Lovell, J., Hermo, L., Claude, A., Melancon, P. and Bergeron, J. J. (1999). Fusogenic domains of golgi membranes are sequestered into specialized regions of the stack that can be released by mechanical fragmentation. J. Cell Biol. 145, 673-688.
    • (1999) J. Cell Biol. , vol.145 , pp. 673-688
    • Dominguez, M.1    Fazel, A.2    Dahan, S.3    Lovell, J.4    Hermo, L.5    Claude, A.6    Melancon, P.7    Bergeron, J.J.8
  • 11
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson, M. J. and Kaiser, C. A. (1996). Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell 7, 1043-1058.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 12
    • 0032988896 scopus 로고    scopus 로고
    • The p24 family of transmembrane proteins at the interface between endoplasmic reticulum and Golgi apparatus
    • Emery, G., Gruenberg, J. and Rojo, M. (1999). The p24 family of transmembrane proteins at the interface between endoplasmic reticulum and Golgi apparatus. Protoplasma 207, 24-30.
    • (1999) Protoplasma , vol.207 , pp. 24-30
    • Emery, G.1    Gruenberg, J.2    Rojo, M.3
  • 13
    • 0033895196 scopus 로고    scopus 로고
    • Coupled transport of p24 family members
    • Emery, G., Rojo, M. and Gruenberg, J. (2000). Coupled transport of p24 family members. J. Cell Sci. 113, 2507-2516.
    • (2000) J. Cell Sci. , vol.113 , pp. 2507-2516
    • Emery, G.1    Rojo, M.2    Gruenberg, J.3
  • 14
    • 0030779039 scopus 로고    scopus 로고
    • Sorting determinants in the transmembrane domain of p24 proteins
    • Fiedler, K. and Rothman, J. E. (1997). Sorting determinants in the transmembrane domain of p24 proteins. J. Biol. Chem. 272, 24739-24742.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24739-24742
    • Fiedler, K.1    Rothman, J.E.2
  • 15
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., Veit, M., Stamnes, M. A. and Rothman, J. E. (1996). Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 17
    • 0039517273 scopus 로고    scopus 로고
    • Localization and recycling of gp27 (hp24gamma3): Complex formation with other p24 family members
    • Fullekrug, J., Suganuma, T., Tang, B. L., Hong, W., Storrie, B. and Nilsson, T. (1999). Localization and recycling of gp27 (hp24gamma3): complex formation with other p24 family members. Mol. Biol. Cell 10, 1939-1955.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1939-1955
    • Fullekrug, J.1    Suganuma, T.2    Tang, B.L.3    Hong, W.4    Storrie, B.5    Nilsson, T.6
  • 19
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • Goldberg, J. (2000). Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 100, 671-679.
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 21
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. (2001). The endocytic pathway: a mosaic of domains. Nat. Rev. Mol. Cell Biol. 2, 721-730.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 22
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • Gu, F., Aniento, F., Parton, R. G. and Gruenberg, J. (1997). Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J. Cell Biol. 139, 1183-1195.
    • (1997) J. Cell Biol. , vol.139 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.G.3    Gruenberg, J.4
  • 23
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P. and Simons, K. (1998). Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141, 929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 24
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • [see comments]
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. and Pease, L. R. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction [see comments]. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 25
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. (2001). Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13, 470-477.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 27
    • 0033942747 scopus 로고    scopus 로고
    • Enrichment of acyl coenzyme A:cholesterol O-acyltransferase near trans- golgi network and endocytic recycling compartment
    • Khelef, N., Soe, T. T., Quebenberger, O., Beatini, N., Tabas, I. and Maxfield, E. R. (2000). Enrichment of acyl coenzyme A:cholesterol O-acyltransferase near trans- golgi network and endocytic recycling compartment. Arterioscler. Thromb. Vasc. Biol. 20, 1769-1776.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1769-1776
    • Khelef, N.1    Soe, T.T.2    Quebenberger, O.3    Beatini, N.4    Tabas, I.5    Maxfield, E.R.6
  • 29
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi, T., Stang, E., Fang, K. S., de Moerloose, P., Parton, R. G. and Gruenberg, J. (1998). A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392, 193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    de Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 31
    • 0033384957 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol
    • Lange, Y., Ye, J., Rigney, M. and Steck, T. L. (1999). Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol. J. Lipid Res. 40, 2264-2270.
    • (1999) J. Lipid Res. , vol.40 , pp. 2264-2270
    • Lange, Y.1    Ye, J.2    Rigney, M.3    Steck, T.L.4
  • 35
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt, A. D. and Hauri, H. P. (1993). Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol. Biol. Cell 4, 679-693.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.P.2
  • 36
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., Donaldson, J. G., Schweizer, A., Berger, E. G., Hauri, H. P., Yuan, L. C. and Klausner, R. D. (1990). Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60, 821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 38
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz, M., Morsomme, P. and Riezman, H. (2001). Protein sorting upon exit from the endoplasmic reticulum. Cell 104, 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 39
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz, M., Nuoffer, C., Hauri, H. P. and Riezman, H. (2000). The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J. Cell Biol. 148, 925-930.
    • (2000) J. Cell Biol. , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 40
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S. (1995). An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14, 4695-4704.
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 41
    • 0037101946 scopus 로고    scopus 로고
    • Vesicular transport: The core machinery of COPI recruitment and budding
    • Nickel, W., Brugger, B. and Wieland, F. T. (2002). Vesicular transport: the core machinery of COPI recruitment and budding. J. Cell Sci. 115, 3235-3240.
    • (2002) J. Cell Sci. , vol.115 , pp. 3235-3240
    • Nickel, W.1    Brugger, B.2    Wieland, F.T.3
  • 42
    • 0027220591 scopus 로고
    • Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok, R., Scheel, J., Horstmann, H., Hauri, H. P., Griffiths, G. and Kreis, T. E. (1993). Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 71-82.
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 43
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • Preuss, D., Mulholland, J., Franzusoff, A., Segev, N. and Botstein, D. (1992). Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell 3, 789-803.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 44
    • 0034033881 scopus 로고    scopus 로고
    • The transmembrane protein p23 contributes to the organization of the Golgi apparatus
    • Rojo, M., Emery, G., Marjomaki, V., McDowall, A. W., Parton, R. G. and Gruenberg, J. (2000). The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J. Cell Sci. 113, 1043-1057.
    • (2000) J. Cell Sci. , vol.113 , pp. 1043-1057
    • Rojo, M.1    Emery, G.2    Marjomaki, V.3    McDowall, A.W.4    Parton, R.G.5    Gruenberg, J.6
  • 46
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O. W., Soderholm, J., Bevis, B. J., Sears, I. B., O'Connor, J., Williamson, E. K. and Glick, B. S. (1999). Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69-81.
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 47
    • 13344280353 scopus 로고    scopus 로고
    • An internalization signal in the simian immunodeficiency virus transmembrane protein cytoplasmic domain modulates expression of envelope glycoproteins on the cell surface
    • Sauter, M. M., Pelchen-Matthews, A., Bron, R., Marsh, M., LaBranche, C. C., Vance, P. J., Romano, J., Haggarty, B. S., Hart, T. K., Lee, W. M. et al. (1996). An internalization signal in the simian immunodeficiency virus transmembrane protein cytoplasmic domain modulates expression of envelope glycoproteins on the cell surface. J. Cell Biol. 132, 795-811.
    • (1996) J. Cell Biol. , vol.132 , pp. 795-811
    • Sauter, M.M.1    Pelchen-Matthews, A.2    Bron, R.3    Marsh, M.4    LaBranche, C.C.5    Vance, P.J.6    Romano, J.7    Haggarty, B.S.8    Hart, T.K.9    Lee, W.M.10
  • 49
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller, F., Singer-Kruger, B., Schroder, S., Kruger, U., Barlowe, C. and Riezman, H. (1995). The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14, 1329-1339.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 50
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., Fransen, J. A., Bachi, T., Ginsel, L. and Hauri, H. P. (1988). Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107, 1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 51
    • 0030943027 scopus 로고    scopus 로고
    • Partitioning of the Golgi apparatus during mitosis in living HeLa cells
    • Shima, D. T., Haldar, K., Pepperkok, R., Watson, R. and Warren, G. (1997). Partitioning of the Golgi apparatus during mitosis in living HeLa cells. J. Cell Biol. 137, 1211-1228.
    • (1997) J. Cell Biol. , vol.137 , pp. 1211-1228
    • Shima, D.T.1    Haldar, K.2    Pepperkok, R.3    Watson, R.4    Warren, G.5
  • 52
    • 0034332917 scopus 로고    scopus 로고
    • Jamming the endosomal system: Lipid rafts and lysosomal storage diseases
    • Simons, K. and Gruenberg, J. (2000). Jamming the endosomal system: lipid rafts and lysosomal storage diseases. Trends Cell Biol. 10, 459-462.
    • (2000) Trends Cell Biol. , vol.10 , pp. 459-462
    • Simons, K.1    Gruenberg, J.2
  • 55
    • 0029147574 scopus 로고
    • An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding
    • [published erratum appears in Proc. Natl. Acad. Sci. USA 1995 Nov 7; 92(23), 10816]
    • Stamnes, M. A., Craighead, M. W., Hoe, M. H., Lampen, N., Geromanos, S., Tempst, P. and Rothman, J. E. (1995). An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding [published erratum appears in Proc. Natl. Acad. Sci. USA 1995 Nov 7; 92(23), 10816]. Proc. Natl. Acad. Sci. USA 92, 8011-8015.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8011-8015
    • Stamnes, M.A.1    Craighead, M.W.2    Hoe, M.H.3    Lampen, N.4    Geromanos, S.5    Tempst, P.6    Rothman, J.E.7
  • 56
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang, E., Kartenbeck, J. and Parton, R. G. (1997). Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol. Biol. Cell 8, 47-57.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 57
    • 0035142512 scopus 로고    scopus 로고
    • The microsporidian Encephalitozoon
    • Vivares, C. P. and Metenier, G. (2001). The microsporidian Encephalitozoon. BioEssays 23, 194-202.
    • (2001) BioEssays , vol.23 , pp. 194-202
    • Vivares, C.P.1    Metenier, G.2
  • 59
    • 0033553858 scopus 로고    scopus 로고
    • p24 proteins and quality control of LIN-12 and GLP-1 trafficking in caenorhabditis elegans
    • Wen, C. and Greenwald, I. (1999). p24 proteins and quality control of LIN-12 and GLP-1 trafficking in caenorhabditis elegans. J. Cell Biol. 145, 1165-1175.
    • (1999) J. Cell Biol. , vol.145 , pp. 1165-1175
    • Wen, C.1    Greenwald, I.2


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