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Volumn 15, Issue 12, 2004, Pages 5538-5550

Regulation of epidermal growth factor receptor degradation by heterotrimeric Gαs protein

Author keywords

[No Author keywords available]

Indexed keywords

DYE; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; G ALPHA S PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; HEPATOCYTE GROWTH FACTOR REGULATED TYROSINE KINASE SUBSTRATE; LIGAND; PROTEIN TYROSINE KINASE; RGS PROTEIN; RGS PX1 PROTEIN; SCATTER FACTOR; TEXAS RED; UNCLASSIFIED DRUG;

EID: 9444263165     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-06-0446     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • Bache, K.G., Brech, A., Mehlum, A., and Stenmark, H. (2003a). Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol. 162, 435-442.
    • (2003) J. Cell Biol. , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 2
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache, K.G., Raiborg, C., Mehlum, A., and Stenmark, H. (2003b). STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278, 12513-12521.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 3
    • 0034714277 scopus 로고    scopus 로고
    • Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome
    • Bao, J., Alroy, I., Waterman, H., Schejter, E.D., Brodie, C., Gruenberg, J., and Yarden, Y. (2000). Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome. J. Biol. Chem. 275, 26178-26186.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26178-26186
    • Bao, J.1    Alroy, I.2    Waterman, H.3    Schejter, E.D.4    Brodie, C.5    Gruenberg, J.6    Yarden, Y.7
  • 4
    • 0028962355 scopus 로고
    • In vitro reconstitution of phagosome-endosome fusion: Evidence for regulation by heterotrimeric GTPases
    • Beron, W., Colombo, M.I., Mayorga, L.S., and Stahl, P.D. (1995). In vitro reconstitution of phagosome-endosome fusion: evidence for regulation by heterotrimeric GTPases. Arch. Biochem. Biophys. 317, 337-342.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 337-342
    • Beron, W.1    Colombo, M.I.2    Mayorga, L.S.3    Stahl, P.D.4
  • 5
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • Bishop, N., Horman, A., and Woodman, P. (2002). Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J. Cell Biol. 157, 91-101.
    • (2002) J. Cell Biol. , vol.157 , pp. 91-101
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 6
    • 0027055668 scopus 로고
    • Role of heterotrimeric G proteins in membrane traffic
    • Bomsel, M. and Mostov, K.E. (1992). Role of heterotrimeric G proteins in membrane traffic. Mol. Biol. Cell 3, 1317-1328.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1317-1328
    • Bomsel, M.1    Mostov, K.E.2
  • 7
    • 0027379648 scopus 로고
    • Possible role of both the alpha and beta gamma subunits of the heterotrimeric G protein, Gs, in transcytosis of the polymeric immunoglobulin receptor
    • Bomsel, M. and Mostov, K.E. (1993). Possible role of both the alpha and beta gamma subunits of the heterotrimeric G protein, Gs, in transcytosis of the polymeric immunoglobulin receptor. J. Biol. Chem. 268, 25824-25835.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25824-25835
    • Bomsel, M.1    Mostov, K.E.2
  • 8
    • 0033860695 scopus 로고    scopus 로고
    • The EGF receptor: A nexus for trafficking and signaling
    • Carpenter, G. (2000). The EGF receptor: a nexus for trafficking and signaling. Bioessays 22, 697-707.
    • (2000) Bioessays , vol.22 , pp. 697-707
    • Carpenter, G.1
  • 9
    • 0035831517 scopus 로고    scopus 로고
    • Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor
    • Chin, L.S., Raynor, M.C., Wei, X., Chen, H.Q., and Li, L. (2001). Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor. J. Biol. Chem. 276, 7069-7078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7069-7078
    • Chin, L.S.1    Raynor, M.C.2    Wei, X.3    Chen, H.Q.4    Li, L.5
  • 10
    • 0242643727 scopus 로고    scopus 로고
    • Hrs function: Viruses provide the clue
    • Clague, M.J. and Urbe, S. (2003). Hrs function: viruses provide the clue. Trends Cell Biol. 13, 603-606.
    • (2003) Trends Cell Biol. , vol.13 , pp. 603-606
    • Clague, M.J.1    Urbe, S.2
  • 11
    • 0026598576 scopus 로고
    • Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion
    • Colombo, M.I., Mayorga, L.S., Casey, P.J., and Stahl, P.D. (1992). Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion. Science 255, 1695-1697.
    • (1992) Science , vol.255 , pp. 1695-1697
    • Colombo, M.I.1    Mayorga, L.S.2    Casey, P.J.3    Stahl, P.D.4
  • 12
    • 0028175798 scopus 로고
    • Gs regulation of endosome fusion suggests a role for signal transduction pathways in endocytosis
    • Colombo, M.I., Mayorga, L.S., Nishimoto, I., Ross, E.M., and Stahl, P.D. (1994). Gs regulation of endosome fusion suggests a role for signal transduction pathways in endocytosis. J. Biol. Chem. 269, 14919-14923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14919-14923
    • Colombo, M.I.1    Mayorga, L.S.2    Nishimoto, I.3    Ross, E.M.4    Stahl, P.D.5
  • 14
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A.C. (1987). G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.C.1
  • 15
    • 0031724592 scopus 로고    scopus 로고
    • Identification of a family of sorting nexin molecules and characterization of their association with receptors
    • Haft, C.R., de la Luz Sierra, M., Barr, V.A., Haft, D.H., and Taylor, S.I. (1998). Identification of a family of sorting nexin molecules and characterization of their association with receptors. Mol. Cell. Biol. 18, 7278-7287.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7278-7287
    • Haft, C.R.1    De La Luz Sierra, M.2    Barr, V.A.3    Haft, D.H.4    Taylor, S.I.5
  • 16
    • 0029116692 scopus 로고
    • Role of heterotrimeric GTP binding proteins in vesicular protein transport: Indications for both classical and alternative G protein cycles
    • Helms, J.B. (1995). Role of heterotrimeric GTP binding proteins in vesicular protein transport: indications for both classical and alternative G protein cycles. FEBS Lett. 369, 84-88.
    • (1995) FEBS Lett. , vol.369 , pp. 84-88
    • Helms, J.B.1
  • 17
    • 2542448950 scopus 로고    scopus 로고
    • Role of mammalian vacuolar protein-sorting proteins in endocytic trafficking of a non-ubiquitinated G protein-coupled receptor to lysosomes
    • Hislop, J.N., Marley, A., and Von Zastrow, M. (2004). role of mammalian vacuolar protein-sorting proteins in endocytic trafficking of a non-ubiquitinated G protein-coupled receptor to lysosomes. J. Biol. Chem. 279, 22522-22531.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22522-22531
    • Hislop, J.N.1    Marley, A.2    Von Zastrow, M.3
  • 18
    • 0036733358 scopus 로고    scopus 로고
    • Cellular regulation of RGS proteins: Modulators and integrators of G protein signaling
    • Hollinger, S. and Hepler, J.R. (2002). Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Pharmacol. Rev. 54, 527-559.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 527-559
    • Hollinger, S.1    Hepler, J.R.2
  • 19
    • 0347093486 scopus 로고    scopus 로고
    • Hrs mediates downregulation of multiple signalling receptors in Drosophila
    • Jekely, G. and Rorth, P. (2003). Hrs mediates downregulation of multiple signalling receptors in Drosophila. EMBO Rep. 4, 1163-1168.
    • (2003) EMBO Rep. , vol.4 , pp. 1163-1168
    • Jekely, G.1    Rorth, P.2
  • 20
  • 21
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann, D.J., Stefan, C.J., Babst, M., and Emr, S.D. (2003). Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162, 413-423.
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 22
    • 0000414462 scopus 로고    scopus 로고
    • A leucine-based determinant in the epidermal growth factor receptor juxtamembrane domain is required for the efficient transport of ligand-receptor complexes to lysosomes
    • Kil, S.J., Hobert, M., and Carlin, C. (1999). A leucine-based determinant in the epidermal growth factor receptor juxtamembrane domain is required for the efficient transport of ligand-receptor complexes to lysosomes. J. Biol. Chem. 274, 3141-3150.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3141-3150
    • Kil, S.J.1    Hobert, M.2    Carlin, C.3
  • 23
    • 0030846562 scopus 로고    scopus 로고
    • Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes
    • Komada, M., Masaki, R., Yamamoto, A., and Kitamura, N. (1997). Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes. J. Biol. Chem. 272, 20538-20544.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20538-20544
    • Komada, M.1    Masaki, R.2    Yamamoto, A.3    Kitamura, N.4
  • 24
    • 0029762883 scopus 로고    scopus 로고
    • Enhanced degradation of EGF receptors by a sorting nexin, SNX1
    • Kurten, R.C., Cadena, D.L., and Gill, G.N. (1996). Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272, 1008-1010.
    • (1996) Science , vol.272 , pp. 1008-1010
    • Kurten, R.C.1    Cadena, D.L.2    Gill, G.N.3
  • 25
    • 0026474549 scopus 로고
    • Activation of the alpha subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity
    • Levis, M.J. and Bourne, H.R. (1992). Activation of the alpha subunit of Gs in intact cells alters its abundance, rate of degradation, and membrane avidity. J. Cell Biol. 119, 1297-1307.
    • (1992) J. Cell Biol. , vol.119 , pp. 1297-1307
    • Levis, M.J.1    Bourne, H.R.2
  • 26
    • 0029658492 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of GSalpha and inhibition of bradykinin-induced activation of the cyclic AMP pathway in A431 cells by epidermal growth factor receptor
    • Liebmann, C., Graness, A., Boehmer, A., Kovalenko, M., Adomeit, A., Steinmetzer, T., Nurnberg, B., Wetzker, R., and Boehmer, F.D. (1996). Tyrosine phosphorylation of GSalpha and inhibition of bradykinin-induced activation of the cyclic AMP pathway in A431 cells by epidermal growth factor receptor. J. Biol. Chem. 271, 31098-31105.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31098-31105
    • Liebmann, C.1    Graness, A.2    Boehmer, A.3    Kovalenko, M.4    Adomeit, A.5    Steinmetzer, T.6    Nurnberg, B.7    Wetzker, R.8    Boehmer, F.D.9
  • 27
    • 0022474869 scopus 로고
    • Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms
    • Lin, C.R., Chen, W.S., Lazar, C.S., Carpenter, C.D., Gill, G.N., Evans, R.M., and Rosenfeld, M.G. (1986). Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms. Cell 44, 839-848.
    • (1986) Cell , vol.44 , pp. 839-848
    • Lin, C.R.1    Chen, W.S.2    Lazar, C.S.3    Carpenter, C.D.4    Gill, G.N.5    Evans, R.M.6    Rosenfeld, M.G.7
  • 28
    • 0000332811 scopus 로고    scopus 로고
    • Sequestration of the G protein beta gamma subunit complex inhibits receptor-mediated endocytosis
    • Lin, H.C., Duncan, J.A., Kozasa, T., and Gilman, A.G. (1998). Sequestration of the G protein beta gamma subunit complex inhibits receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 95, 5057-5060.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5057-5060
    • Lin, H.C.1    Duncan, J.A.2    Kozasa, T.3    Gilman, A.G.4
  • 29
    • 0037596749 scopus 로고    scopus 로고
    • TSG101 interaction with HRS mediates endosomal trafficking and receptor downregulation
    • Lu, Q., Hope, L.W., Brasch, M., Reinhard, C., and Cohen, S.N. (2003). TSG101 interaction with HRS mediates endosomal trafficking and receptor downregulation. Proc. Natl. Acad. Sci. USA 100, 7626-7631.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7626-7631
    • Lu, Q.1    Hope, L.W.2    Brasch, M.3    Reinhard, C.4    Cohen, S.N.5
  • 30
    • 0242362743 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4
    • Marchese, A., Raiborg, C., Santini, F., Keen, J.H., Stenmark, H., and Benovic, J.L. (2003). The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4. Dev. Cell 5, 709-722.
    • (2003) Dev. Cell , vol.5 , pp. 709-722
    • Marchese, A.1    Raiborg, C.2    Santini, F.3    Keen, J.H.4    Stenmark, H.5    Benovic, J.L.6
  • 31
    • 0026690840 scopus 로고
    • Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein
    • McConnen, S.J., and Yaffe, M.P. (1992). Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein. J. Cell Biol. 118, 385-395.
    • (1992) J. Cell Biol. , vol.118 , pp. 385-395
    • McConnen, S.J.1    Yaffe, M.P.2
  • 32
    • 0025572744 scopus 로고
    • Gs alpha mediates epidermal growth factor-elicited stimulation of rat cardiac adenylate cyclase
    • Nair, B.G., Parikh, B., Milligan, G., and Patel, T.B. (1990). Gs alpha mediates epidermal growth factor-elicited stimulation of rat cardiac adenylate cyclase. J. Biol. Chem. 265, 21317-21322.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21317-21322
    • Nair, B.G.1    Parikh, B.2    Milligan, G.3    Patel, T.B.4
  • 33
    • 0037205055 scopus 로고    scopus 로고
    • G protein pathways
    • Neves, S.R., Ram, P.T., and Iyengar, R. (2002). G protein pathways. Science 296, 1636-1639.
    • (2002) Science , vol.296 , pp. 1636-1639
    • Neves, S.R.1    Ram, P.T.2    Iyengar, R.3
  • 34
    • 0030600131 scopus 로고    scopus 로고
    • Potential roles of heterotrimeric G proteins of the endomembrane system
    • Nurnberg, B., and Ahnert-Hilger, G. (1996). Potential roles of heterotrimeric G proteins of the endomembrane system. FEBS Lett. 389, 61-65.
    • (1996) FEBS Lett. , vol.389 , pp. 61-65
    • Nurnberg, B.1    Ahnert-Hilger, G.2
  • 35
    • 0029664393 scopus 로고    scopus 로고
    • Activation of Gsalpha by the epidermal growth factor receptor involves phosphorylation
    • Poppleton, H., Sun, H., Fulgham, D., Bertics, P., and Patel, T.B. (1996). Activation of Gsalpha by the epidermal growth factor receptor involves phosphorylation. J. Biol. Chem. 271, 6947-6951.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6947-6951
    • Poppleton, H.1    Sun, H.2    Fulgham, D.3    Bertics, P.4    Patel, T.B.5
  • 37
    • 0034941051 scopus 로고    scopus 로고
    • FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
    • Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D.J., D'Arrigo, A., Stang, E., and Stenmark, H. (2001b). FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114, 2255-2263.
    • (2001) J. Cell Sci. , vol.114 , pp. 2255-2263
    • Raiborg, C.1    Bremnes, B.2    Mehlum, A.3    Gillooly, D.J.4    D'Arrigo, A.5    Stang, E.6    Stenmark, H.7
  • 39
    • 0037005404 scopus 로고    scopus 로고
    • Hrs and endocytic sorting of ubiquitinated membrane proteins
    • Raiborg, C. and Stenmark, H. (2002). Hrs and endocytic sorting of ubiquitinated membrane proteins. Cell Struct. Funct. 27, 403-408.
    • (2002) Cell Struct. Funct. , vol.27 , pp. 403-408
    • Raiborg, C.1    Stenmark, H.2
  • 40
    • 0343079334 scopus 로고
    • Stimulation of beta-adrenergic receptors of S49 lymphoma cells redistributes the alpha subunit of the stimulatory G protein between cytosol and membranes
    • Ransnas, L.A., Svoboda, P., Jasper, J.R., and Insel, P.A. (1989). Stimulation of beta-adrenergic receptors of S49 lymphoma cells redistributes the alpha subunit of the stimulatory G protein between cytosol and membranes. Proc. Natl. Acad. Sci. USA 86, 7900-7903.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7900-7903
    • Ransnas, L.A.1    Svoboda, P.2    Jasper, J.R.3    Insel, P.A.4
  • 41
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • Sachse, M., Urbe, S., Oorschot, V., Strous, G.J., and Klumperman, J. (2002). Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell 13, 1313-1328.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1313-1328
    • Sachse, M.1    Urbe, S.2    Oorschot, V.3    Strous, G.J.4    Klumperman, J.5
  • 42
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: Close encounters of many kinds
    • Sorkin, A. and Von Zastrow, M. (2002). Signal transduction and endocytosis: close encounters of many kinds. Nat. Rev. Mol. Cell. Biol. 3, 600-614.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 600-614
    • Sorkin, A.1    Von Zastrow, M.2
  • 43
    • 12544250585 scopus 로고    scopus 로고
    • Multivesicular bodies and multivesicular endosomes: The "ins and outs" of endosomal traffic
    • Stahl, P.D. and Barbieri, M.A. (2002). Multivesicular bodies and multivesicular endosomes: the "ins and outs" of endosomal traffic. Sci STKE 2002, PE32.
    • (2002) Sci STKE , vol.2002
    • Stahl, P.D.1    Barbieri, M.A.2
  • 44
    • 0032516854 scopus 로고    scopus 로고
    • Vesicle budding on Golgi membranes: Regulation by G proteins and myosin motors
    • Stow, J.L. and Heimann, K. (1998). Vesicle budding on Golgi membranes: regulation by G proteins and myosin motors. Biochim. Biophys. Acta 1404, 161-171.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 161-171
    • Stow, J.L.1    Heimann, K.2
  • 45
    • 0031041588 scopus 로고    scopus 로고
    • The juxtamembrane, cytosolic region of the epidermal growth factor receptor is involved in association with alpha-subunit of Gs
    • Sun, H., Chen, Z., Poppleton, H., Scholich, K., Mullenix, J., Weipz, G.J., Fulgham, D.L., Bertics, P.J., and Patel, T.B. (1997). The juxtamembrane, cytosolic region of the epidermal growth factor receptor is involved in association with alpha-subunit of Gs. J. Biol. Chem. 272, 5413-5420.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5413-5420
    • Sun, H.1    Chen, Z.2    Poppleton, H.3    Scholich, K.4    Mullenix, J.5    Weipz, G.J.6    Fulgham, D.L.7    Bertics, P.J.8    Patel, T.B.9
  • 46
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • Sun, W., Yan, Q., Vida, T.A., and Bean, A.J. (2003). Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J. Cell Biol. 162, 125-137.
    • (2003) J. Cell Biol. , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 48
    • 2942650512 scopus 로고    scopus 로고
    • Heterotrimeric G protein subunits are located on rat liver endosomes
    • Van Dyke, R.W. (2004). Heterotrimeric G protein subunits are located on rat liver endosomes. BMC Physiol. 4, 1.
    • (2004) BMC Physiol. , vol.4 , pp. 1
    • Van Dyke, R.W.1
  • 49
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A. and Emr, S.D. (1995). A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128, 779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 50
    • 0028173706 scopus 로고
    • Activation and depalmitoylation of Gs alpha
    • Wedegaertner, P.B. and Bourne, H.R. (1994). Activation and depalmitoylation of Gs alpha. Cell 77, 1063-1070.
    • (1994) Cell , vol.77 , pp. 1063-1070
    • Wedegaertner, P.B.1    Bourne, H.R.2
  • 51
    • 0029779537 scopus 로고    scopus 로고
    • Activation-induced subcellular redistribution of Gs alpha
    • Wedegaertner, P.B., Bourne, H.R., and von Zastrow, M. (1996). Activation-induced subcellular redistribution of Gs alpha. Mol. Biol. Cell 7, 1225-1233.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1225-1233
    • Wedegaertner, P.B.1    Bourne, H.R.2    Von Zastrow, M.3
  • 52
    • 0035967888 scopus 로고    scopus 로고
    • Phoxy lipids, revealing PX domains as phosphoinositide binding modules
    • Wishart, M.J., Taylor, G.S., and Dixon, J.E. (2001). Phoxy lipids, revealing PX domains as phosphoinositide binding modules. Cell 105, 817-820.
    • (2001) Cell , vol.105 , pp. 817-820
    • Wishart, M.J.1    Taylor, G.S.2    Dixon, J.E.3
  • 53
    • 0036904274 scopus 로고    scopus 로고
    • Sorting out the cellular functions of sorting nexins
    • Worby, C.A. and Dixon, J.E. (2002). Sorting out the cellular functions of sorting nexins. Nat. Rev. Mol. Cell. Biol. 3, 919-931.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 919-931
    • Worby, C.A.1    Dixon, J.E.2
  • 54
    • 9444230586 scopus 로고    scopus 로고
    • Ca2+ and NSF differentially regulate disassembly of SNARE complexes on early endosomes
    • Yan, Q., Sun, W., McNew, J.A., Vida, T.A., and Bean, A.J. (2004). Ca2+ and NSF differentially regulate disassembly of SNARE complexes on early endosomes. J. Biol. Chem.
    • (2004) J. Biol. Chem.
    • Yan, Q.1    Sun, W.2    McNew, J.A.3    Vida, T.A.4    Bean, A.J.5
  • 55
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate
    • Yu, J.W. and Lemmon, M.A. (2001). All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J. Biol. Chem. 276, 44179-44184.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2
  • 56
    • 0036151483 scopus 로고    scopus 로고
    • Real-time visualization of a fluorescent G(alpha)(s): Dissociation of the activated G protein from plasma membrane
    • Yu, J.Z. and Rasenick, M.M. (2002). Real-time visualization of a fluorescent G(alpha)(s): dissociation of the activated G protein from plasma membrane. Mol. Pharmacol. 61, 352-359.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 352-359
    • Yu, J.Z.1    Rasenick, M.M.2
  • 57
    • 0034635962 scopus 로고    scopus 로고
    • MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16
    • Zheng, B., Chen, D., and Farquhar, M.G. (2000). MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc. Natl. Acad. Sci. USA 97, 3999-4004.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3999-4004
    • Zheng, B.1    Chen, D.2    Farquhar, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.