메뉴 건너뛰기




Volumn 20, Issue 7, 2009, Pages 1937-1948

Vps41 phosphorylation and the rab ypt7 control the targeting of the HOPS complex to Endosome-Vacuole fusion Sites

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; MUTANT PROTEIN; PROTEIN HOPS; PROTEIN SUBUNIT; PROTEIN VPS41; RAB PROTEIN; RAB YPT7 PROTEIN; UNCLASSIFIED DRUG;

EID: 65249126973     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-09-0943     Document Type: Article
Times cited : (79)

References (37)
  • 1
    • 0033584946 scopus 로고    scopus 로고
    • Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition
    • Albert, S., and Gallwitz, D.(1999). Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition. J. Biol. Chem. 274, 33186 -33189.
    • (1999) J. Biol. Chem , vol.274 , pp. 33186-33189
    • Albert, S.1    Gallwitz, D.2
  • 2
    • 65249143958 scopus 로고    scopus 로고
    • Genome- wide analysis of AP-3 dependent protein transport in yeast
    • Anand, V. C., Daboussi, L., Lorenz, T. C., and Payne, G. S.(2009). Genome- wide analysis of AP-3 dependent protein transport in yeast. Mol. Biol. Cell 20, 1592-1604.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1592-1604
    • Anand, V.C.1    Daboussi, L.2    Lorenz, T.C.3    Payne, G.S.4
  • 3
    • 0037128929 scopus 로고    scopus 로고
    • Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p
    • Bonangelino, C. J., Nau, J. J., Duex, J. E., Brinkman, M., Wurmser, A. E., Gary, J. D., Emr, S. D., and Weisman, L. S.(2002). Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p. J. Cell Biol. 156, 1015-1028.
    • (2002) J. Cell Biol , vol.156 , pp. 1015-1028
    • Bonangelino, C.J.1    Nau, J.J.2    Duex, J.E.3    Brinkman, M.4    Wurmser, A.E.5    Gary, J.D.6    Emr, S.D.7    Weisman, L.S.8
  • 4
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos, J. L., Rehmann, H., and Wittinghofer, A.(2007). GEFs and GAPs: critical elements in the control of small G proteins. Cell 129, 865-877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 5
    • 52249085200 scopus 로고    scopus 로고
    • Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase
    • Brett,C. L.,Plemel,R. L.,Lobinger,B. T.,Vignali,M.,Fields,S.,and Merz,A. J.(2008). Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J. Cell Biol. 182, 1141-1151.
    • (2008) J. Cell Biol , vol.182 , pp. 1141-1151
    • Brett, C.L.1    Plemel, R.L.2    Lobinger, B.T.3    Vignali, M.4    Fields, S.5    Merz, A.J.6
  • 6
    • 34247623568 scopus 로고    scopus 로고
    • Cai, H., Reinisch, K., and Ferro-Novick, S.(2007). Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671-682.
    • Cai, H., Reinisch, K., and Ferro-Novick, S.(2007). Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671-682.
  • 7
    • 43249126878 scopus 로고    scopus 로고
    • Asymmetric tethering of flat and curved lipid membranes by a golgin
    • Drin, G., Morello, V., Casella, J. F., Gounon, P., and Antonny, B.(2008). Asymmetric tethering of flat and curved lipid membranes by a golgin. Science 320, 670-673.
    • (2008) Science , vol.320 , pp. 670-673
    • Drin, G.1    Morello, V.2    Casella, J.F.3    Gounon, P.4    Antonny, B.5
  • 8
    • 46349104022 scopus 로고    scopus 로고
    • A cryosectioning procedure for the ultrastructural analysis and the immunogold labelling of yeast Saccharomyces cerevisiae
    • Griffith, J., Mari, M., De Maziere, A., and Reggiori, F.(2008). A cryosectioning procedure for the ultrastructural analysis and the immunogold labelling of yeast Saccharomyces cerevisiae. Traffic 9, 1060-1072.
    • (2008) Traffic , vol.9 , pp. 1060-1072
    • Griffith, J.1    Mari, M.2    De Maziere, A.3    Reggiori, F.4
  • 9
    • 0032213106 scopus 로고    scopus 로고
    • Casein kinase I: Spatial organization and positioning of a multifunctional protein kinase family
    • Gross, S. D., and Anderson, R. A.(1998). Casein kinase I: spatial organization and positioning of a multifunctional protein kinase family. Cell Signal. 10, 699-711.
    • (1998) Cell Signal , vol.10 , pp. 699-711
    • Gross, S.D.1    Anderson, R.A.2
  • 10
    • 0001199243 scopus 로고
    • A quantitative assay to measure homotypic vacuole fusion in vitro
    • Haas, A.(1995). A quantitative assay to measure homotypic vacuole fusion in vitro. Methods Cell Sci. 17, 283-294.
    • (1995) Methods Cell Sci , vol.17 , pp. 283-294
    • Haas, A.1
  • 11
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H., and Emr, S. D.(2006). The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu. Rev. Biophys. Biomol. Struct. 35, 277-298.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 12
    • 4444271170 scopus 로고    scopus 로고
    • Janke, C., et al.(2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21, 947-962.
    • Janke, C., et al.(2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21, 947-962.
  • 13
    • 13444251066 scopus 로고    scopus 로고
    • The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex
    • LaGrassa, T. J., and Ungermann, C.(2005). The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex. J. Cell Biol. 168, 401-414.
    • (2005) J. Cell Biol , vol.168 , pp. 401-414
    • LaGrassa, T.J.1    Ungermann, C.2
  • 14
    • 34248175894 scopus 로고    scopus 로고
    • Conformational changes of coat proteins during vesicle formation
    • Langer, J. D., Stoops, E. H., Bethune, J., and Wieland, F. T.(2007). Conformational changes of coat proteins during vesicle formation. FEBS Lett. 581, 2083-2088.
    • (2007) FEBS Lett , vol.581 , pp. 2083-2088
    • Langer, J.D.1    Stoops, E.H.2    Bethune, J.3    Wieland, F.T.4
  • 15
    • 36649027300 scopus 로고    scopus 로고
    • Trypanosoma brucei vacuolar protein sorting 41(VPS41) is required for intracellular iron utilization and maintenance of normal cellular morphology
    • Lu, S., Suzuki, T., Iizuka, N., Ohshima, S., Yabu, Y., Suzuki, M., Wen, L., and Ohta, N.(2007). Trypanosoma brucei vacuolar protein sorting 41(VPS41) is required for intracellular iron utilization and maintenance of normal cellular morphology. Parasitology 134, 1639-1647.
    • (2007) Parasitology , vol.134 , pp. 1639-1647
    • Lu, S.1    Suzuki, T.2    Iizuka, N.3    Ohshima, S.4    Yabu, Y.5    Suzuki, M.6    Wen, L.7    Ohta, N.8
  • 16
    • 34248227351 scopus 로고    scopus 로고
    • Rab cascades and tethering factors in the endomembrane system
    • Markgraf, D. F., Peplowska, K., and Ungermann, C.(2007). Rab cascades and tethering factors in the endomembrane system. FEBS Lett. 581, 2125-2130.
    • (2007) FEBS Lett , vol.581 , pp. 2125-2130
    • Markgraf, D.F.1    Peplowska, K.2    Ungermann, C.3
  • 17
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p(NSF)-driven release of Sec17p(alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W., and Haas, A.(1996). Sec18p(NSF)-driven release of Sec17p(alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 18
    • 1642539980 scopus 로고    scopus 로고
    • Trans-SNARE interactions elicit Ca2 + efflux from the yeast vacuole lumen
    • Merz, A. J., and Wickner, W. T.(2004). Trans-SNARE interactions elicit Ca2 + efflux from the yeast vacuole lumen. J. Cell Biol. 164, 195-206.
    • (2004) J. Cell Biol , vol.164 , pp. 195-206
    • Merz, A.J.1    Wickner, W.T.2
  • 19
    • 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., and Wada, Y.(1997). 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) J. Biol. Chem , vol.272 , pp. 11344-11349
    • Nakamura, N.1    Hirata, A.2    Ohsumi, Y.3    Wada, Y.4
  • 20
    • 38049029618 scopus 로고    scopus 로고
    • Yeast vacuole fusion: A model system for eukaryotic endomembrane dynamics
    • Ostrowicz, C. W., Meiringer, C. T., and Ungermann, C.(2008). Yeast vacuole fusion: a model system for eukaryotic endomembrane dynamics. Autophagy 4, 5-19.
    • (2008) Autophagy , vol.4 , pp. 5-19
    • Ostrowicz, C.W.1    Meiringer, C.T.2    Ungermann, C.3
  • 21
    • 34247568898 scopus 로고    scopus 로고
    • The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis
    • Peplowska, K., Markgraf, D. F., Ostrowicz, C. W., Bange, G., and Ungermann, C.(2007). The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev. Cell 12, 739-750.
    • (2007) Dev. Cell , vol.12 , pp. 739-750
    • Peplowska, K.1    Markgraf, D.F.2    Ostrowicz, C.W.3    Bange, G.4    Ungermann, C.5
  • 22
    • 15544382255 scopus 로고    scopus 로고
    • Kinases regulating Golgi apparatus structure and function
    • Preisinger, C., and Barr, F. A.(2005). Kinases regulating Golgi apparatus structure and function. Biochem. Soc. Symp. 15-30.
    • (2005) Biochem. Soc. Symp , pp. 15-30
    • Preisinger, C.1    Barr, F.A.2
  • 23
    • 0032531048 scopus 로고    scopus 로고
    • New constructs and strategies for efficient PCR-based gene manipulations in yeast
    • Puig, O., Rutz, B., Luukkonen, B. G., Kandels-Lewis, S., Bragado-Nilsson, E., and Seraphin, B.(1998). New constructs and strategies for efficient PCR-based gene manipulations in yeast. Yeast 14, 1139-1146.
    • (1998) Yeast , vol.14 , pp. 1139-1146
    • Puig, O.1    Rutz, B.2    Luukkonen, B.G.3    Kandels-Lewis, S.4    Bragado-Nilsson, E.5    Seraphin, B.6
  • 24
    • 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
  • 25
    • 0033739781 scopus 로고    scopus 로고
    • Polar transmembrane domains target proteins to the interior of the yeast vacuole
    • Reggiori, F., Black, M. W., and Pelham, H. R.(2000). Polar transmembrane domains target proteins to the interior of the yeast vacuole. Mol. Biol. Cell. 11, 3737-3749.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3737-3749
    • Reggiori, F.1    Black, M.W.2    Pelham, H.R.3
  • 26
    • 0033202889 scopus 로고    scopus 로고
    • Formation of AP-3 transport intermediates requires Vps41 function
    • Rehling, P., Darsow, T., Katzmann, D. J., and Emr, S. D.(1999). Formation of AP-3 transport intermediates requires Vps41 function. Nat. Cell Biol. 1, 346353.
    • (1999) Nat. Cell Biol , vol.1 , pp. 346353
    • Rehling, P.1    Darsow, T.2    Katzmann, D.J.3    Emr, S.D.4
  • 27
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • 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 vacuolar protein sorting mutant. 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
  • 28
    • 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., and Emr, S. D.(1997). 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) Mol. Biol. Cell , vol.8 , pp. 2307-2327
    • Rieder, S.E.1    Emr, S.D.2
  • 29
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Seraphin, B.(1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032.
    • (1999) Nat. Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 30
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • Rink, J., Ghigo, E., Kalaidzidis, Y., and Zerial, M.(2005). Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735-749.
    • (2005) Cell , vol.122 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 31
    • 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., and Price, A.(2000). 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) 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
  • 32
    • 48749099702 scopus 로고    scopus 로고
    • HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion
    • Starai, V. J., Hickey, C. M., and Wickner, W.(2008). HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion. Mol. Biol. Cell. 19, 2500-2508.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2500-2508
    • Starai, V.J.1    Hickey, C.M.2    Wickner, W.3
  • 33
    • 33646128965 scopus 로고    scopus 로고
    • Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p
    • Stroupe, C., Collins, K. M., Fratti, R. A., and Wickner, W.(2006). Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J. 25, 1579-1589.
    • (2006) EMBO J , vol.25 , pp. 1579-1589
    • Stroupe, C.1    Collins, K.M.2    Fratti, R.A.3    Wickner, W.4
  • 34
    • 1542344019 scopus 로고    scopus 로고
    • The yeast casein kinase Yck3p is palmitoylated, then sorted to the vacuolar membrane with AP-3-dependent recognition of a YXXPhi adaptin sorting signal
    • Sun, B., Chen, L., Cao, W., Roth, A. F., and Davis, N. G.(2004). The yeast casein kinase Yck3p is palmitoylated, then sorted to the vacuolar membrane with AP-3-dependent recognition of a YXXPhi adaptin sorting signal. Mol. Biol. Cell. 15, 1397-1406.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1397-1406
    • Sun, B.1    Chen, L.2    Cao, W.3    Roth, A.F.4    Davis, N.G.5
  • 35
    • 0037415612 scopus 로고    scopus 로고
    • Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
    • Wang, L., Merz, A. J., Collins, K. M., and Wickner, W.(2003). Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J. Cell Biol. 160, 365-374.
    • (2003) J. Cell Biol , vol.160 , pp. 365-374
    • Wang, L.1    Merz, A.J.2    Collins, K.M.3    Wickner, W.4
  • 36
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte, J. R., and Munro, S.(2002). Vesicle tethering complexes in membrane traffic. J. Cell Sci. 115, 2627-2637.
    • (2002) J. Cell Sci , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 37
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the ypt7 GT- Pase to SNARE-dependent docking and fusion
    • Wurmser, A. E., Sato, T. K., and Emr, S. D.(2000). New component of the vacuolar class C-Vps complex couples nucleotide exchange on the ypt7 GT- Pase to SNARE-dependent docking and fusion. J. Cell Biol. 151, 551-562.
    • (2000) J. Cell Biol , vol.151 , pp. 551-562
    • Wurmser, A.E.1    Sato, T.K.2    Emr, S.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.