메뉴 건너뛰기




Volumn 17, Issue 11, 1998, Pages 2982-2993

The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function

Author keywords

ATPase; Endosome; Transport; Vacuole

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DIMER; MEMBRANE PROTEIN;

EID: 0032101334     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.11.2982     Document Type: Article
Times cited : (647)

References (55)
  • 1
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • Arlt, H., Tauer, R., Feldmann, H., Neupert, W. and Langer, T. (1996) The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell, 85, 875-885.
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 2
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., Sato, T.K., Banta, L.M. and Emr, S.E. (1997) Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J., 16, 1820-1831.
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.E.4
  • 3
    • 0030012162 scopus 로고    scopus 로고
    • Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast
    • Becherer, K.A., Reider, S., Emr, S.D. and Jones, E.W. (1996) Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast. Mol. Biol. Cell, 7, 579-594.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 579-594
    • Becherer, K.A.1    Reider, S.2    Emr, S.D.3    Jones, E.W.4
  • 4
    • 0024366928 scopus 로고
    • Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein
    • Beckers, C.J., Block, M.R., Glick, B.S., Rothman, J.E. and Balch, W.E. (1989) Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein. Nature, 339, 397-398.
    • (1989) Nature , vol.339 , pp. 397-398
    • Beckers, C.J.1    Block, M.R.2    Glick, B.S.3    Rothman, J.E.4    Balch, W.E.5
  • 5
    • 0030867609 scopus 로고    scopus 로고
    • Sequence analysis of the AAA protein family
    • Beyer, A. (1997) Sequence analysis of the AAA protein family. Protein Sci., 6, 2043-2058.
    • (1997) Protein Sci. , vol.6 , pp. 2043-2058
    • Beyer, A.1
  • 6
    • 0030797279 scopus 로고    scopus 로고
    • Syntaxin 6 functions in trans-Golgi network vesicle trafficking
    • Bock, J.B., Klumperman, J., Davanger, S. and Scheller, R.H. (1997) Syntaxin 6 functions in trans-Golgi network vesicle trafficking. Mol. Biol. Cell, 8, 1261-1271.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1261-1271
    • Bock, J.B.1    Klumperman, J.2    Davanger, S.3    Scheller, R.H.4
  • 7
    • 0029977573 scopus 로고    scopus 로고
    • A yeast protein related to a mammalian Ras-binding protein, Vps9p, is required for localization of vacuolar proteins
    • Burd, C.G., Mustol, P.A., Schu, P.V. and Emr, S.D. (1996) A yeast protein related to a mammalian Ras-binding protein, Vps9p, is required for localization of vacuolar proteins. Mol. Cell. Biol., 16, 2369-2377.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2369-2377
    • Burd, C.G.1    Mustol, P.A.2    Schu, P.V.3    Emr, S.D.4
  • 8
    • 0030952211 scopus 로고    scopus 로고
    • A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast
    • Burd, C.G., Peterson, M., Cowles, C.R. and Emr, S.D. (1997) A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast. Mol. Biol. Cell, 8, 1089-1104.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1089-1104
    • Burd, C.G.1    Peterson, M.2    Cowles, C.R.3    Emr, S.D.4
  • 9
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function and localization
    • Cereghino, J.L., Marcusson, E.G. and Emr, S.D. (1995) The cytoplasmic tail domain of the vacuolar sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function and localization. Mol. Biol. Cell, 6, 1089-1102.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 11
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F. and Duguet, M. (1995) A 200-amino acid ATPase module in search of a basic function. BioEssays, 17, 639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 12
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component epsilon-COP
    • Daro, E., Sheff, D., Gomez, M., Kreis, T. and Mellman, I. (1997) Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component epsilon-COP. J. Cell Biol., 139, 1747-1759.
    • (1997) J. Cell Biol. , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.4    Mellman, I.5
  • 13
    • 0021913292 scopus 로고
    • Assembly of the mitochondrial membrane system. CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b
    • Dieckmann, C.L. and Tzagoloff, A. (1985) Assembly of the mitochondrial membrane system. CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b. J. Biol. Chem., 260, 1513-1520.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1513-1520
    • Dieckmann, C.L.1    Tzagoloff, A.2
  • 14
    • 1842299354 scopus 로고    scopus 로고
    • The VPS4 gene is involved in protein transport out of a yeast pre-vacuolar endosome-like compartment
    • Finken-Eigen, M., Rohricht, R.A. and Kohrer, K. (1997) The VPS4 gene is involved in protein transport out of a yeast pre-vacuolar endosome-like compartment. Curr. Genet., 31, 469-480.
    • (1997) Curr. Genet. , vol.31 , pp. 469-480
    • Finken-Eigen, M.1    Rohricht, R.A.2    Kohrer, K.3
  • 15
    • 0028881024 scopus 로고
    • The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM
    • Frohlich, K.U., Fries, H.W., Peters, J.M. and Mecke, D. (1995) The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM. Biochim. Biophys. Acta, 1253, 25-32.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 25-32
    • Frohlich, K.U.1    Fries, H.W.2    Peters, J.M.3    Mecke, D.4
  • 16
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T.R. and Emr, S.D. (1991) Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol., 114, 207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 17
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J. and Maxfield, F. (1995) Membrane transport in the endocytic pathway. Curr. Opin. Cell Biol., 7, 552-563.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.2
  • 18
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R. and Heuser, J.E. (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell, 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 19
  • 20
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J.C. and Scheller, R.H. (1997) SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol., 9, 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 21
    • 0030803426 scopus 로고    scopus 로고
    • Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/ N-ethylmaleimide-sensitive fusion protein
    • Hicke, L., Zanolari, B., Pypaert, M., Rohrer, J., Riezman, H., TerBush, D.R., Maurice, T., Roth, D. and Novick, P. (1997) Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/ N-ethylmaleimide-sensitive fusion protein. Mol. Biol. Cell, 8, 13-31.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 13-31
    • Hicke, L.1    Zanolari, B.2    Pypaert, M.3    Rohrer, J.4    Riezman, H.5    TerBush, D.R.6    Maurice, T.7    Roth, D.8    Novick, P.9
  • 22
    • 0027418058 scopus 로고
    • The VPS16 gene product associates with a sedimentable protein complex and is essential for vacuolar protein sorting in yeast
    • Horazdovsky, B.F. and Emr, S.D. (1993) The VPS16 gene product associates with a sedimentable protein complex and is essential for vacuolar protein sorting in yeast. J. Biol. Chem., 268, 4953-4962.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4953-4962
    • Horazdovsky, B.F.1    Emr, S.D.2
  • 23
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 24
    • 0017600514 scopus 로고
    • Proteinase mutants of Saccharomyces cerevisiae
    • Jones, E.W. (1977) Proteinase mutants of Saccharomyces cerevisiae. Genetics, 85, 23-33.
    • (1977) Genetics , vol.85 , pp. 23-33
    • Jones, E.W.1
  • 25
    • 0028264403 scopus 로고
    • Regulatory role of major tyrosine autophosphorylation site of kinase domain of c-Met receptor (scatter factor/hepatocyte growth factor receptor)
    • Komada, M. and Kitamura, N. (1994) Regulatory role of major tyrosine autophosphorylation site of kinase domain of c-Met receptor (scatter factor/hepatocyte growth factor receptor). J. Biol. Chem., 269, 16131-16136.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16131-16136
    • Komada, M.1    Kitamura, N.2
  • 26
    • 0030846562 scopus 로고    scopus 로고
    • Hrs, a tyrosine kinase substrate with a conserved double zinc ringer 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 ringer 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
  • 27
    • 0026632366 scopus 로고
    • Evidence for ADP-ribosylation factor (ARF) as a regulator of in vitro endosome-endosome fusion
    • Lenhard, J.M., Kahn, R.A. and Stahl, P.D. (1992) Evidence for ADP-ribosylation factor (ARF) as a regulator of in vitro endosome-endosome fusion. J. Biol. Chem., 267, 13047-13052.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13047-13052
    • Lenhard, J.M.1    Kahn, R.A.2    Stahl, P.D.3
  • 28
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M. and Stock, J. (1991) Predicting coiled coils from protein sequences. Science, 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 29
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 30
    • 0030809132 scopus 로고    scopus 로고
    • Domain structure and intramolecular regulation of dynamin GTPase
    • Muhlberg, A.B., Warnock, D.E. and Schmid, S.L. (1997) Domain structure and intramolecular regulation of dynamin GTPase. EMBO J., 16, 6676-6683.
    • (1997) EMBO J. , vol.16 , pp. 6676-6683
    • Muhlberg, A.B.1    Warnock, D.E.2    Schmid, S.L.3
  • 31
    • 0030989278 scopus 로고    scopus 로고
    • Rab7 regulates transport from early to late endocytic compartments in Xenopus oocytes
    • Mukhopadhyay, A., Funato, K. and Stahl, P.D. (1997) Rab7 regulates transport from early to late endocytic compartments in Xenopus oocytes. J. Biol. Chem., 272, 13055-13059.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13055-13059
    • Mukhopadhyay, A.1    Funato, K.2    Stahl, P.D.3
  • 32
    • 0028802295 scopus 로고
    • Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A. and Whiteheart, S.W. (1995) Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem., 270, 29182-29188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 33
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P. and Zerial, M. (1997) The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol., 9, 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 34
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S. and Latterich, M. (1998) The AAA team: related ATPases with diverse functions. Trends Cell Biol., 8, 65-71.
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 35
    • 0028017842 scopus 로고
    • Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast
    • Perier, F. Coulter, K.L., Liang, H., Radeke, C.M., Gaber, R.F. and Vandenberg, C.A. (1994) Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast. FEBS Lett., 351, 286-290.
    • (1994) FEBS Lett. , vol.351 , pp. 286-290
    • Perier, F.1    Coulter, K.L.2    Liang, H.3    Radeke, C.M.4    Gaber, R.F.5    Vandenberg, C.A.6
  • 36
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters, J.M., Walsh, M.J. and Franke, W.W. (1990) An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J., 9, 1757-1767.
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 37
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R.C., Cooper, A.A., Yang, H. and Stevens, T.H. (1995) VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell. Biol., 131, 603-618.
    • (1995) J. Cell. Biol. , vol.131 , pp. 603-618
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 38
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class e vps mutants
    • Raymond, C.K., Howald-Stevenson, I., Vater, C.A. and Stevens, T.H. (1992) Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell, 3, 1389-1402.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 39
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome like compartment accumulates in the yeast vps28
    • Rieder, S.E., Banta, L.M., Kohrer, K., McCaffery, J.M. and Emr, S.D. (1996) Multilamellar endosome like compartment accumulates in the yeast vps28. Mol. Biol. Cell, 7, 985-999.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 985-999
    • Rieder, S.E.1    Banta, L.M.2    Kohrer, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 40
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., Klionsky, D.J., Banta, L.M. and Emr, S.D. (1988) Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell. Biol., 8, 4936-4948.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 41
    • 0030827050 scopus 로고    scopus 로고
    • NSF is required for transport from early to late endosomes
    • Robinson, L.J., Aniento, F. and Gruenberg, J. (1997) NSF is required for transport from early to late endosomes. J. Cell Sci., 110, 2079-2087.
    • (1997) J. Cell Sci. , vol.110 , pp. 2079-2087
    • Robinson, L.J.1    Aniento, F.2    Gruenberg, J.3
  • 42
    • 0028142717 scopus 로고
    • Multiple N-ethylmaleimide-sensitive components are required for endosomal vesicle fusion
    • Rodriguez, L., Stirling, C.J. and Woodman, P.G. (1994) Multiple N-ethylmaleimide-sensitive components are required for endosomal vesicle fusion. Mol. Biol. Cell, 5, 773-783.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 773-783
    • Rodriguez, L.1    Stirling, C.J.2    Woodman, P.G.3
  • 43
    • 0024445121 scopus 로고
    • Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae
    • Rothman, J.H., Howald, I. and Stevens, T.H. (1989) Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae. EMBO J., 8, 2057-2065.
    • (1989) EMBO J. , vol.8 , pp. 2057-2065
    • Rothman, J.H.1    Howald, I.2    Stevens, T.H.3
  • 48
    • 0031452311 scopus 로고    scopus 로고
    • Mutational analysis of Csc1/Vps4p: Involvement of endosome in regulation of autophagy in yeast
    • Shirahama, K., Noda, T. and Ohsumi, Y. (1997) Mutational analysis of Csc1/Vps4p: involvement of endosome in regulation of autophagy in yeast. Cell Struct. Funct., 22, 501-509.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 501-509
    • Shirahama, K.1    Noda, T.2    Ohsumi, Y.3
  • 49
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof, T.C. (1995) The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature, 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 50
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γ S in nerve terminals
    • Takei, K., McPherson, P.S., Schmid, S.L. and De Camilli, P. (1995) Tubular membrane invaginations coated by dynamin rings are induced by GTP-γ S in nerve terminals. Nature, 374, 186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 51
    • 0027302761 scopus 로고
    • Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae
    • Tu, J., Vallier, L.G. and Carlson, M. (1993) Molecular and genetic analysis of the SNF7 gene in Saccharomyces cerevisiae. Genetics, 135, 17-23.
    • (1993) Genetics , vol.135 , pp. 17-23
    • Tu, J.1    Vallier, L.G.2    Carlson, M.3
  • 52
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M. and Parton, R.G. (1996) Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol., 135, 913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 53
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • Warnock, D.E., Hinshaw, J.E. and Schmid, S.L. (1996) Dynamin self-assembly stimulates its GTPase activity. J. Biol. Chiem., 271, 22310-22314.
    • (1996) J. Biol. Chiem. , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 54
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S.W., Rossnagel, K., Buhrow, S.A., Brunner, M., Jaenicke, R. and Rothman, J.E. (1994) N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol., 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 55
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney, J.A., Gomez, M., Sheff, D., Kreis, T.E. and Mellman, I. (1995) Cytoplasmic coat proteins involved in endosome function. Cell, 83, 703-713.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.