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Volumn 2, Issue 2, 2001, Pages 107-117

Rab proteins as membrane organizers

Author keywords

[No Author keywords available]

Indexed keywords

RAB PROTEIN;

EID: 0035257013     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35052055     Document Type: Review
Times cited : (2809)

References (105)
  • 1
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. Mechanisms of intracellular protein transport. Nature 372, 55-63 (1994).
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 2
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T. et al. SNAREpins: minimal machinery for membrane fusion. Cell 92, 759-772 (1998).
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1
  • 3
    • 0034648836 scopus 로고    scopus 로고
    • Compartmental specificity of cellular membrane fusion encoded in SNARE proteins
    • McNew, J. A. et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407, 153-159 (2000). Using the reconstituted liposome fusion assay, Rothman and colleagues systematically tested liposomes containing each of the yeast v-SNAREs for fusion with three potential t-SNARE complexes. The cognate SNARE pairs showed a high degree of selectivity, an important tenant of the SNARE hypothesis.
    • (2000) Nature , vol.407 , pp. 153-159
    • McNew, J.A.1
  • 4
    • 0034648797 scopus 로고    scopus 로고
    • Topological restriction of SNARE-dependent membrane fusion
    • Parlati, F. et al. Topological restriction of SNARE-dependent membrane fusion. Nature 407, 194-198 (2000).
    • (2000) Nature , vol.407 , pp. 194-198
    • Parlati, F.1
  • 5
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P. & Zerial, M. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9, 496-504 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 6
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N. & Barlowe, C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17, 2156-2165 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 7
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • Allan, B. B., Moyer, B. D. & Balch, W. E. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 289, 444-448 (2000). Shows that the previously identified tethering factor, p115, is a Rab1 effector and direct ly interacts with the SNARE machinery. The functional importance of an interaction between a Rab effector and the cis-SNARE complex during vesicle budding highlights the multiple roles of Rab effectors.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 8
    • 0034599993 scopus 로고    scopus 로고
    • Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes
    • Cao, X. & Barlowe, C. Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes. J. Cell Biol. 149, 55-66 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 55-66
    • Cao, X.1    Barlowe, C.2
  • 9
    • 0032080081 scopus 로고    scopus 로고
    • TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion
    • Sacher, M. et al. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. EMBO J. 17, 2494-2503 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2494-2503
    • Sacher, M.1
  • 10
    • 0034676094 scopus 로고    scopus 로고
    • TRAPP stimulates guanine nucleotide exchange on Ypt1p
    • Wang, W., Sacher, M. & Ferro-Novick, S. TRAPP stimulates guanine nucleotide exchange on Ypt1p. J. Cell Biol. 151, 289-296 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 289-296
    • Wang, W.1    Sacher, M.2    Ferro-Novick, S.3
  • 11
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush, D. R., Maurice, T., Roth, D. & Novick, P. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15, 6483-6494 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 12
    • 0031447173 scopus 로고    scopus 로고
    • Subunit structure of the mammalian exocyst complex
    • Kee, Y. et al. Subunit structure of the mammalian exocyst complex. Proc. Natl Acad. Sci. USA 94, 14438-14443 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14438-14443
    • Kee, Y.1
  • 13
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger, F. P., Hughes, T. E. & Novick, P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92, 559-571 (1998). Exocytosis in yeast occurs in a polarized fashion. This study shows that Sec3p localizes to the site of polarized exocytosis and Is required for the targeting of secretory vesicles to the bud. This is in line with the concept that Rab effectors specify where the vesicles should tether on their target compartment, allowing trans-SNARE complex formation to mediate fusion.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 14
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo, W., Roth, D., Walch-Solimena, C. & Novick, P. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18, 1071-1080 (1999). This work established that Sec15p, a subunit of the exocyst, is a Sec4p effector protein. It supports the idea that Rab proteins regulate the function of multimeric protein complexes important in the initial recognition of the docking site for an incoming vesicle.
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 15
    • 0025974686 scopus 로고
    • Rab5 controls early endosome fusion in vitro
    • Gorvel, J. -P., Chavrier, P., Zerial, M. & Gruenberg, J. Rab5 controls early endosome fusion in vitro. Cell 64, 915-925 (1991).
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 16
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C. et al. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70, 715-728 (1992).
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1
  • 17
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Chistoforidis, S., McBride, H. M., Burgoyne, R., D. & Zerial, M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621-625 (1999). The identification of over 20 proteins that bind specifically to activated Rab5 opened up the idea that a much more complex protein machinery could be downstream of a Rab protein and have a wider regulatory role than previously imagined. Second, this paper shows that EEA1 alone can tether early endosomes and allow the SNARE machinery to mediate fusion.
    • (1999) Nature , vol.397 , pp. 621-625
    • Chistoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 18
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links phosphatidylinositol 3-kinase function to RabS regulation of endosome fusion
    • Simonsen, A. et al. EEA1 links phosphatidylinositol 3-kinase function to RabS regulation of endosome fusion. Nature 394, 494-498 (1998).
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1
  • 19
    • 0032476057 scopus 로고    scopus 로고
    • Evidence for a symmetrical requirement for Rab5-GTP in in vitro endosome-endosome fusion
    • Barbieri, M. A. et al. Evidence for a symmetrical requirement for Rab5-GTP in in vitro endosome-endosome fusion. J. Biol. Chem. 273, 25850-25855 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 25850-25855
    • Barbieri, M.A.1
  • 20
    • 0034635387 scopus 로고    scopus 로고
    • Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes
    • Rubino, M., Miaczynska, M., Lippe, R. & Zerial, M. Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. J. Biol. Chem. 275, 3745-3748 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3745-3748
    • Rubino, M.1    Miaczynska, M.2    Lippe, R.3    Zerial, M.4
  • 21
    • 0028788311 scopus 로고
    • The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance
    • Haas, A., Scheglmann, D., Lazar, T., Gallwitz, D. & Wickner, W. The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance. EMBO J. 14, 5258-5270 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5258-5270
    • Haas, A.1    Scheglmann, D.2    Lazar, T.3    Gallwitz, D.4    Wickner, W.5
  • 22
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. & Wickner, W. Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 23
    • 0030830765 scopus 로고    scopus 로고
    • A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole
    • Rieder, S. E. & Emr, S. D. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol. Biol. Cell 8, 2307-2327 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2307-2327
    • Rieder, S.E.1    Emr, S.D.2
  • 24
    • 0034689024 scopus 로고    scopus 로고
    • The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein
    • Price, A., Seals, D., Wickner, W. & Ungermann, C. The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J. Cell Boil. 148, 1231-1238 (2000). These experiments have shown that the HOPS complex is an effector of Ypt7p in vacuole tethering. Furthermore, this work, together with References 57 and 86 provided the first demonstrations of the dynamics of the interactions between Rab effector and SNARE machineries.
    • (2000) J. Cell Boil. , vol.148 , pp. 1231-1238
    • Price, A.1    Seals, D.2    Wickner, W.3    Ungermann, C.4
  • 25
    • 0034662876 scopus 로고    scopus 로고
    • A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • Seals, D. F., Eitzen, G., Margolis, N., Wickner, W. T. & Price, A. A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc. Natl Acad. Sci. USA 97, 9402-9407 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.5
  • 26
    • 0034689021 scopus 로고    scopus 로고
    • Proteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion
    • Price, A., Wickner, W. & Ungermann, C. Proteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion. J. Cell Biol. 148, 1223-1230 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 1223-1230
    • Price, A.1    Wickner, W.2    Ungermann, C.3
  • 27
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser, A. E., Sato, T. K. & Emr, S. D. New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J. Cell Biol. 151, 551-562 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3
  • 28
    • 17344377424 scopus 로고    scopus 로고
    • A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function
    • Horiuchi, H. et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 90, 1149-1159 (1997).
    • (1997) Cell , vol.90 , pp. 1149-1159
    • Horiuchi, H.1
  • 29
    • 0028181701 scopus 로고
    • A GDP-bound form of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments
    • Nuoffer, C., Davidson, H. W., Matteson, J., Meinkoth, J. & Balch, W. E. A GDP-bound form of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments. J. Cell Biol. 125, 225-237 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 225-237
    • Nuoffer, C.1    Davidson, H.W.2    Matteson, J.3    Meinkoth, J.4    Balch, W.E.5
  • 30
    • 0028224561 scopus 로고
    • Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans Golgi network
    • Riederer, M. A., Soldati, T., Shapiro, A. D., Lin, J. & Pfeffer, S. Lysosome biogenesis requires Rab9 function and receptor recycling from endosomes to the trans Golgi network. J. Cell Biol. 125, 573-582 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 573-582
    • Riederer, M.A.1    Soldati, T.2    Shapiro, A.D.3    Lin, J.4    Pfeffer, S.5
  • 31
    • 0028233498 scopus 로고
    • COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum
    • Barlowe, C. et al. COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77, 895-907 (1994).
    • (1994) Cell , vol.77 , pp. 895-907
    • Barlowe, C.1
  • 32
    • 0031983836 scopus 로고    scopus 로고
    • A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits
    • McLauchlan, H. et al. A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits. Cure Biol. 8, 34-45 (1998).
    • (1998) Cure Biol. , vol.8 , pp. 34-45
    • McLauchlan, H.1
  • 33
    • 0034676451 scopus 로고    scopus 로고
    • The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5
    • Lanzetti, L. et al. The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5. Nature 408, 374-377 (2000).
    • (2000) Nature , vol.408 , pp. 374-377
    • Lanzetti, L.1
  • 34
    • 0033202889 scopus 로고    scopus 로고
    • Formation of AP-3 transport intermediates requires Vps41 function
    • Rehling, P., Darsow, T., Katzmann, D. J. & Emr, S. D. Formation of AP-3 transport intermediates requires Vps41 function. Nature Cell Biol. 1, 346-353 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 346-353
    • Rehling, P.1    Darsow, T.2    Katzmann, D.J.3    Emr, S.D.4
  • 35
    • 0032559265 scopus 로고    scopus 로고
    • Interaction of a Golgi-associated kinesin-like protein with Rab6
    • Echard, A. et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science 279, 580-585 (1998). A yeast two-hybrid search for effectors identified a kinesin as a Rab6-interacting protein. In line with the concept that Rab proteins can have different functions, this result suggests that a Rab protein might be functionally connected with the microtubule-dependent motility of vesicles and organelles.
    • (1998) Science , vol.279 , pp. 580-585
    • Echard, A.1
  • 36
    • 0034331310 scopus 로고    scopus 로고
    • The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis
    • Hill, E., Clarke, M. & Barr, F. A. The Rab6-binding kinesin, Rab6-KIFL, is required for cytokinesis. EMBO J. 19, 5711-5719 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5711-5719
    • Hill, E.1    Clarke, M.2    Barr, F.A.3
  • 37
    • 0033202945 scopus 로고    scopus 로고
    • Rab5 regulates motility of early endosomes on microtubules
    • Nielsen, E., Severin, F., Backer, J. M., Hyman, A. A. & Zerial, M. Rab5 regulates motility of early endosomes on microtubules. Nature Cell Biol. 1, 376-382 (1999). A role of Rab5 in the attachment and motility of early endosomes along microtubules was uncovered using in vitro assays. These data together with the findings of Reference 35, strongly support an additional role of Rab proteins in organelle movement along the cytoskeleton.
    • (1999) Nature Cell Biol. , vol.1 , pp. 376-382
    • Nielsen, E.1    Severin, F.2    Backer, J.M.3    Hyman, A.A.4    Zerial, M.5
  • 38
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne, D. W., Schott, D. H. & Bretscher, A. Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J. Cell Biol. 143, 1931-1945 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 39
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott, D., Ho, J., Pruyne, D. & Bretscher, A. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 147, 791-808 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 791-808
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 40
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Menasche, G. et al. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nature Genet. 25, 173-176 (2000).
    • (2000) Nature Genet. , vol.25 , pp. 173-176
    • Menasche, G.1
  • 41
    • 0025967015 scopus 로고
    • Novel myosin heavy chain encoded by murine dilute coat colour locus
    • erratum 352, 547 (1992)
    • Mercer, J. A., Seperack, P. K., Strobel, M. C., Copeland, N. G. & Jenkins, N. A. Novel myosin heavy chain encoded by murine dilute coat colour locus. Nature 349, 709-713 (1991); erratum 352, 547 (1992).
    • (1991) Nature , vol.349 , pp. 709-713
    • Mercer, J.A.1    Seperack, P.K.2    Strobel, M.C.3    Copeland, N.G.4    Jenkins, N.A.5
  • 42
    • 12944255844 scopus 로고    scopus 로고
    • A mutation in Rab27a causes the vesicle transport defects observed in ashen mice
    • Wilson, S. M. et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc. Natl Acad. Sci. USA 97, 7933-7938 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7933-7938
    • Wilson, S.M.1
  • 43
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase RabS in endocytic membrane fusion
    • Stenmark, H., Vitale, G., Ullrich, O. & Zerial, M. Rabaptin-5 is a direct effector of the small GTPase RabS in endocytic membrane fusion. Cell 83, 423-432 (1995).
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 44
    • 0029822793 scopus 로고    scopus 로고
    • GTPase activity of RabS acts as a timer for endocytic membrane fusion
    • Rybin, V. et al. GTPase activity of RabS acts as a timer for endocytic membrane fusion. Nature 383, 266-269 (1996).
    • (1996) Nature , vol.383 , pp. 266-269
    • Rybin, V.1
  • 45
    • 0029846518 scopus 로고    scopus 로고
    • Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger
    • Stenmark, H., Aasland, R., Toh, B. H. & D'Arrigo, A. Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger. J. Biol. Chem. 271, 24048-24054 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 24048-24054
    • Stenmark, H.1    Aasland, R.2    Toh, B.H.3    D'Arrigo, A.4
  • 46
    • 0033492236 scopus 로고    scopus 로고
    • FYVE-finger proteins - Effectors of an inositol lipid
    • Stenmark, H. & Aasland, R. FYVE-finger proteins - effectors of an inositol lipid. J. Cell Sci. 112, 4175-4183 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 4175-4183
    • Stenmark, H.1    Aasland, R.2
  • 47
    • 0034602964 scopus 로고    scopus 로고
    • The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization
    • Lawe, D. C., Patki, V., Heller-Harrison, R., Lambright, D. & Corvera, S. The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization. J. Biol. Chem. 275, 3699-3705 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3699-3705
    • Lawe, D.C.1    Patki, V.2    Heller-Harrison, R.3    Lambright, D.4    Corvera, S.5
  • 48
    • 0033174034 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-OH kinases are RabS effectors
    • Christoforidis, S. et al. Phosphatidylinositol-3-OH kinases are RabS effectors. Nature Cell Biol. 1, 249-252 (1999). The identification of two distinct lipid kinases as effectors of a Rab protein linked the Rab field to signal transduction and strengthened the idea that Rabs regulate the assembly of specialized lipid and protein microdomains.
    • (1999) Nature Cell Biol. , vol.1 , pp. 249-252
    • Christoforidis, S.1
  • 50
    • 0033605718 scopus 로고    scopus 로고
    • The role of phosphoinositide 3-kinase lipid products in cell function
    • Rameh, L. E. & Cantley, L. C. The role of phosphoinositide 3-kinase lipid products in cell function. J. Biol. Chem. 274, 8347-8350 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8347-8350
    • Rameh, L.E.1    Cantley, L.C.2
  • 51
    • 0032517624 scopus 로고    scopus 로고
    • Distinct roles for the p110α and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis
    • Siddhanta, U., McIlroy, J., Shah, A., Zhang, Y. & Backer, J. M. Distinct roles for the p110α and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis. J. Cell Biol. 143, 1647-1659 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1647-1659
    • Siddhanta, U.1    McIlroy, J.2    Shah, A.3    Zhang, Y.4    Backer, J.M.5
  • 52
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu, P. V. et al. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260, 88-91 (1993). First demonstration of a functional connection between PI(3)K and membrane transport.
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1
  • 53
    • 0028981018 scopus 로고
    • A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system
    • Volinia, S. et al. A human phosphatidylinositol 3-kinase complex related to the yeast Vps34p-Vps15p protein sorting system. EMBO J. 14, 3339-3348 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3339-3348
    • Volinia, S.1
  • 54
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd, C. G. & Emr, S. D. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell 2, 157-162 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 55
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • Gillooly, D. J. et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19, 4577-4588 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4577-4588
    • Gillooly, D.J.1
  • 56
    • 0034735512 scopus 로고    scopus 로고
    • Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain
    • Nielsen, E. et al. Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J. Cell Biol. 151, 601-612 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 601-612
    • Nielsen, E.1
  • 57
    • 0033840979 scopus 로고    scopus 로고
    • EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts
    • Wilson, J. M. et al. EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts. Mol. Biol. Cell 11, 2657-2671 (2000). References 57, 68-70 support the Idea that Rab proteins and their effectors are compartmentalized in early endosomes and show a non-random distribution.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2657-2671
    • Wilson, J.M.1
  • 58
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride, H. M. et al. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98, 377-386 (1999).
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1
  • 59
    • 0034157389 scopus 로고    scopus 로고
    • Role of membrane organization and membrane domains in endocytic lipid trafficking
    • Mukherjiee, S. & Maxfield, F. R. Role of membrane organization and membrane domains in endocytic lipid trafficking. Traffic 1, 203-211 (2000).
    • (2000) Traffic , vol.1 , pp. 203-211
    • Mukherjiee, S.1    Maxfield, F.R.2
  • 60
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. & Ikonen, E. Functional rafts in cell membranes. Nature 387, 569-572 (1997).
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 61
    • 0034697119 scopus 로고    scopus 로고
    • The class II phosphoinositide 3-kinase PI3K-C2α is concentrated in the trans-Golgi network and present in clathrin-coated vesicles
    • Domin, J., Gaidarov, I., Smith, M. E., Keen, J. H. & Waterfield, M. D. The class II phosphoinositide 3-kinase PI3K-C2α is concentrated in the trans-Golgi network and present in clathrin-coated vesicles. J. Biol. Chem. 275, 11943-11950 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 11943-11950
    • Domin, J.1    Gaidarov, I.2    Smith, M.E.3    Keen, J.H.4    Waterfield, M.D.5
  • 62
    • 0032168684 scopus 로고    scopus 로고
    • Phosphoinositide signaling and turnover: Ptdlns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities
    • Wurmser, A. E. & Emr, S. D. Phosphoinositide signaling and turnover: Ptdlns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities. EMBO J. 17, 4930-4942 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4930-4942
    • Wurmser, A.E.1    Emr, S.D.2
  • 63
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for Ptdlns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary, J. D., Wurmser, A. E., Bonangelino, C. J., Weisman, L. S. & Emr, S. D. Fab1p is essential for Ptdlns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis. J. Cell Biol. 143, 65-79 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 64
    • 0034703432 scopus 로고    scopus 로고
    • Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway
    • Blondeau, F. et al. Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. Hum. Mol. Genet. 9, 2223-2229 (2000).
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2223-2229
    • Blondeau, F.1
  • 65
    • 0032145247 scopus 로고    scopus 로고
    • The role of ankyrin and spectrin in membrane transport and domain formation
    • De Matteis, M. A. & Morrow, J. S. The role of ankyrin and spectrin in membrane transport and domain formation. Curr. Opin. Cell Biol. 10, 542-549 (1998).
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 542-549
    • De Matteis, M.A.1    Morrow, J.S.2
  • 66
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter, J. et al. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18, 4949-4960 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4949-4960
    • Shorter, J.1
  • 67
    • 0000804465 scopus 로고    scopus 로고
    • Endosome fusion in living cells overexpressing GFP-rab5
    • Roberts, R. L. et al. Endosome fusion in living cells overexpressing GFP-rab5. J. Cell Sci. 112, 3667-3675 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 3667-3675
    • Roberts, R.L.1
  • 68
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen, B., De Renzis, S., Nielsen, E., Rietdorf, J. & Zerial, M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J. Cell Biol. 149, 901-914 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 69
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff, D. R., Daro, E. A., Hull, M. & Mellman, I. The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145, 123-139 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 70
    • 0033379104 scopus 로고    scopus 로고
    • Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway
    • Trischler, M., Stoorvogel, W. & Ullrich, O. Biochemical analysis of distinct Rab5-and Rab11-positive endosomes along the transferrin pathway. J. Cell Sci. 112, 4773-4783 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 4773-4783
    • Trischler, M.1    Stoorvogel, W.2    Ullrich, O.3
  • 71
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J. & Maxfield, F. R. Membrane transport in the endocytic pathway. Curr. Opin. Cell Biol. 7, 552-563 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 72
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway
    • van der Sluijs, P. et al. The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell 70, 729-740 (1992).
    • (1992) Cell , vol.70 , pp. 729-740
    • Van Der Sluijs, P.1
  • 73
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbé, S., Zerial, M. & Parton, R. G. Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbé, S.3    Zerial, M.4    Parton, R.G.5
  • 74
    • 0032055405 scopus 로고    scopus 로고
    • Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5
    • Vitale, G. et al. Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5. EMBO J. 17, 1941-1951 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1941-1951
    • Vitale, G.1
  • 75
    • 0034332917 scopus 로고    scopus 로고
    • Jamming the endosomal system: Lipid rafts and lysosomal storage diseases
    • Simons, K. & Gruenberg, J. Jamming the endosomal system: lipid rafts and lysosomal storage diseases. Trends Cell Biol. 10, 459-462 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 459-462
    • Simons, K.1    Gruenberg, J.2
  • 76
    • 0032175908 scopus 로고    scopus 로고
    • Novel pathways, membrane coats and Pl kinase regulation in yeast lysosomal trafficking
    • Burd, C. G., Babst, M. & Emr, S. D. Novel pathways, membrane coats and Pl kinase regulation in yeast lysosomal trafficking. Semin. Cell Dev. Biol. 9, 527-533 (1998).
    • (1998) Semin. Cell Dev. Biol. , vol.9 , pp. 527-533
    • Burd, C.G.1    Babst, M.2    Emr, S.D.3
  • 77
    • 0030940407 scopus 로고    scopus 로고
    • Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae
    • Nakamura, N., Hirata, A., Ohsumi, Y. & Wada, Y. Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 272, 11344-11349 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 11344-11349
    • Nakamura, N.1    Hirata, A.2    Ohsumi, Y.3    Wada, Y.4
  • 78
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff, K. K. et al. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93, 731-740 (1998).
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1
  • 80
    • 0033558032 scopus 로고    scopus 로고
    • The sec6/8 complex is located at neunte outgrowth and axonal synapse-assembly domains
    • Hazuka, C. D. et al. The sec6/8 complex is located at neunte outgrowth and axonal synapse-assembly domains. J. Neurosci. 19, 1324-1334 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 1324-1334
    • Hazuka, C.D.1
  • 81
    • 0033571602 scopus 로고    scopus 로고
    • Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells
    • White, J. et al. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J. Cell Biol. 147, 743-760 (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 743-760
    • White, J.1
  • 82
    • 0027932454 scopus 로고
    • Specificity and regulation of a synaptic vesicle docking complex
    • Pevsner, J. et al. Specificity and regulation of a synaptic vesicle docking complex. Neuron 13, 353-361 (1994).
    • (1994) Neuron , vol.13 , pp. 353-361
    • Pevsner, J.1
  • 84
    • 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. & Emr, S. D. A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast. Mol. Biol. Cell 8, 1089-1104 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1089-1104
    • Burd, C.G.1    Peterson, M.2    Cowles, C.R.3    Emr, S.D.4
  • 85
    • 0033545389 scopus 로고    scopus 로고
    • Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome
    • Peterson, M. R., Burd, C. G. & Emr, S. D. Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome. Curr. Biol. 9, 159-162 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 159-162
    • Peterson, M.R.1    Burd, C.G.2    Emr, S.D.3
  • 86
    • 0032978370 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting
    • Tall, G. G., Hama, H., DeWald, D. B. & Horazdovsky, B. F. The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol. Biol. Cell 10, 1873-1889 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1873-1889
    • Tall, G.G.1    Hama, H.2    DeWald, D.B.3    Horazdovsky, B.F.4
  • 87
    • 0033634646 scopus 로고    scopus 로고
    • Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion
    • Sato, T. K., Rehling, P., Peterson, M. R. & Emr, S. D. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol. Cell 6, 661-671 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 661-671
    • Sato, T.K.1    Rehling, P.2    Peterson, M.R.3    Emr, S.D.4
  • 88
    • 0032478142 scopus 로고    scopus 로고
    • Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
    • Orci, L., Perrelet, A. & Rothman, J. E. Vesicles on strings: morphological evidence for processive transport within the Golgi stack. Proc. Natl Acad Sci. USA 95, 2279-2283 (1998).
    • (1998) Proc. Natl Acad Sci. USA , vol.95 , pp. 2279-2283
    • Orci, L.1    Perrelet, A.2    Rothman, J.E.3
  • 89
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C. & Skehel, J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56, 365-394 (1987).
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 90
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda, T. Q., Abramson, P. D. & Spudich, J. A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Natl Acad Sci. USA 93, 4459-4464 (1996).
    • (1996) Proc. Natl Acad Sci. USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 91
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • Howard, J. & Spudich, J. A. Is the lever arm of myosin a molecular elastic element? Proc. Natl Acad. Sci. USA 93, 4462-4464 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 92
    • 0034616174 scopus 로고    scopus 로고
    • Motility powered by supramolecular springs and ratchets
    • Mahadevan, L. & Matsudaira, P. Motility powered by supramolecular springs and ratchets. Science 288, 95-100 (2000).
    • (2000) Science , vol.288 , pp. 95-100
    • Mahadevan, L.1    Matsudaira, P.2
  • 93
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M. I., Beron, W. & Stahl, P. D. Calmodulin regulates endosome fusion. J. Biol. Chem. 272, 7707-7712 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 94
    • 0346605832 scopus 로고    scopus 로고
    • Rab33B regulates intra-Golgi transport and utilizes a novel kinesin as an effector
    • Abstract no. 1244, 214a Washington, D. C.
    • Koda, T., Zheng, J. Y. & Ishibe, M. Rab33B regulates intra-Golgi transport and utilizes a novel kinesin as an effector. 39th Annual Meeting of the American Society for Cell Biology Abstract no. 1244, 214a (Washington, D. C., 1999).
    • (1999) 39th Annual Meeting of the American Society for Cell Biology
    • Koda, T.1    Zheng, J.Y.2    Ishibe, M.3
  • 95
    • 0031712806 scopus 로고    scopus 로고
    • Rho and Rab small G proteins coordinately reorganize stress fibers and focal adhesions in MDCK cells
    • Imamura, H. et al. Rho and Rab small G proteins coordinately reorganize stress fibers and focal adhesions in MDCK cells. Mol. Biol. Cell 9, 2561-2575 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2561-2575
    • Imamura, H.1
  • 96
    • 0033180113 scopus 로고    scopus 로고
    • The role of ARF and Rab GTPases in membrane transport
    • Chavrier, P. & Goud, B. The role of ARF and Rab GTPases in membrane transport. Curr. Opin. Cell Biol. 11, 466-475 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 466-475
    • Chavrier, P.1    Goud, B.2
  • 97
    • 0031023505 scopus 로고    scopus 로고
    • Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI
    • Dirac-Svejstrup, A. B., Sumizawa, T. & Pfeffer, S. R. Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J. 16, 465-472 (1997).
    • (1997) EMBO J. , vol.16 , pp. 465-472
    • Dirac-Svejstrup, A.B.1    Sumizawa, T.2    Pfeffer, S.R.3
  • 98
    • 0030835887 scopus 로고    scopus 로고
    • Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosome membranes
    • Ayad, N., Hull, M. & Mellman, I. Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosome membranes. EMBO J. 16, 4497-4507 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4497-4507
    • Ayad, N.1    Hull, M.2    Mellman, I.3
  • 99
    • 0033583815 scopus 로고    scopus 로고
    • Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1)
    • Bucci, C., Chiariello, M., Lattero, D., Maiorano, M. & Bruni, C. B. Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1). Biochem. Biophys. Res. Commun. 258, 657-662 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 657-662
    • Bucci, C.1    Chiariello, M.2    Lattero, D.3    Maiorano, M.4    Bruni, C.B.5
  • 100
    • 0034282521 scopus 로고    scopus 로고
    • A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting
    • Matern, H. et al. A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting. EMBO J. 19, 4485-4492 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4485-4492
    • Matern, H.1
  • 101
    • 0034637447 scopus 로고    scopus 로고
    • A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion
    • Hoffenberg, S. et al. A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion. J. Biol. Chem. 275, 24661-24669 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24661-24669
    • Hoffenberg, S.1
  • 102
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved α-helical peripheral membrane protein flanked by cysteine 'fingers' and contains a calmodulin-binding IQ motif
    • Mu, F. T. et al. EEA1, an early endosome-associated protein. EEA1 is a conserved α-helical peripheral membrane protein flanked by cysteine 'fingers' and contains a calmodulin-binding IQ motif. J. Biol. Chem. 270, 13503-13511 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13503-13511
    • Mu, F.T.1
  • 104
    • 0033606766 scopus 로고    scopus 로고
    • Sec1p binds to SNARE complexes and concentrates at sites of secretion
    • Carr, C. M., Grote, E., Munson, M., Hughson, F. M. & Novick, P. J. Sec1p binds to SNARE complexes and concentrates at sites of secretion. J. Cell Biol. 146, 333-344 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 333-344
    • Carr, C.M.1    Grote, E.2    Munson, M.3    Hughson, F.M.4    Novick, P.J.5
  • 105
    • 0032879685 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 interacts directly with syntaxin-6
    • Simonsen, A., Gaullier, J. M., D'Arrigo, A. & Stenmark, H. The Rab5 effector EEA1 interacts directly with syntaxin-6. J. Biol. Chem. 274, 28857-28860 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28857-28860
    • Simonsen, A.1    Gaullier, J.M.2    D'Arrigo, A.3    Stenmark, H.4


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