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Volumn 192, Issue 2, 2011, Pages 295-306

Bro1 binding to Snf7 regulates ESCRT-III membrane scission activity in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ESCRT PROTEIN; PROTEIN; PROTEIN BRO 1; PROTEIN SNF 7; UNCLASSIFIED DRUG;

EID: 78951470141     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201007018     Document Type: Article
Times cited : (71)

References (53)
  • 1
    • 33747375410 scopus 로고    scopus 로고
    • Interaction of AMSH with ESCR-TIII and deubiquitination of endosomal cargo
    • doi:10.1074/jbc.M513803200
    • Agromayor, M., and J. Martin-Serrano. 2006. Interaction of AMSH with ESCR-TIII and deubiquitination of endosomal cargo. J. Biol. Chem. 281:23083-23091. doi:10.1074/jbc.M513803200
    • (2006) J. Biol. Chem. , vol.281 , pp. 23083-23091
    • Agromayor, M.1    Martin-Serrano, J.2
  • 2
    • 33644525938 scopus 로고    scopus 로고
    • Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1
    • doi:10.1083/jcb.200508166
    • Azmi, I., B. Davies, C. Dimaano, J. Payne, D. Eckert, M. Babst, and D.J. Katzmann. 2006. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J. Cell Biol. 172:705-717. doi:10.1083/jcb. 200508166
    • (2006) J. Cell Biol. , vol.172 , pp. 705-717
    • Azmi, I.1    Davies, B.2    Dimaano, C.3    Payne, J.4    Eckert, D.5    Babst, M.6    Katzmann, D.J.7
  • 3
    • 37749048772 scopus 로고    scopus 로고
    • ESCR-TIII family members stimulate Vps4 ATPase activity directly or via Vta1
    • doi:10.1016/j.devcel.2007.10.021
    • Azmi, I.F., B.A. Davies, J. Xiao, M. Babst, Z. Xu, and D.J. Katzmann. 2008. ESCR-TIII family members stimulate Vps4 ATPase activity directly or via Vta1. Dev. Cell. 14:50-61. doi:10.1016/j.devcel.2007.10.021
    • (2008) Dev. Cell , vol.14 , pp. 50-61
    • Azmi, I.F.1    Davies, B.A.2    Xiao, J.3    Babst, M.4    Xu, Z.5    Katzmann, D.J.6
  • 4
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • doi:10.1093/emboj/16.8.1820
    • Babst, M., T.K. Sato, L.M. Banta, and S.D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831. doi:10.1093/emboj/16.8.1820
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 5
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • doi:10.1093/emboj/17.11.2982
    • Babst, M., B. Wendland, E.J. Estepa, and S.D. Emr. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993. doi:10.1093/emboj/17.11.2982
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 6
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • doi:10.1016/S1534-5807(02)00219-8
    • Babst, M., D.J. Katzmann, W.B. Snyder, B. Wendland, and S.D. Emr. 2002. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell. 3:283-289. doi:10.1016/S1534- 5807(02)00219-8
    • (2002) Dev. Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 7
    • 1642373357 scopus 로고    scopus 로고
    • Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae
    • doi:10.1111/j.1600-0854.2004.00169.x
    • Bowers, K., J. Lottridge, S.B. Helliwell, L.M. Goldthwaite, J.P. Luzio, and T.H. Stevens. 2004. Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic. 5:194-210. doi:10.1111/j.1600-0854. 2004.00169.x
    • (2004) Traffic , vol.5 , pp. 194-210
    • Bowers, K.1    Lottridge, J.2    Helliwell, S.B.3    Goldthwaite, L.M.4    Luzio, J.P.5    Stevens, T.H.6
  • 8
    • 34347385894 scopus 로고    scopus 로고
    • Parallels between cytokinesis and retroviral budding: A role for the ESCRT machinery
    • doi:10.1126/science.1143422
    • Carlton, J.G., and J. Martin-Serrano. 2007. Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science. 316:1908-1912. doi:10.1126/science.1143422
    • (2007) Science , vol.316 , pp. 1908-1912
    • Carlton, J.G.1    Martin-Serrano, J.2
  • 9
    • 48749119362 scopus 로고    scopus 로고
    • Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release
    • doi:10.1073/pnas.0802008105
    • Carlton, J.G., M. Agromayor, and J. Martin-Serrano. 2008. Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release. Proc. Natl. Acad. Sci. USA. 105:10541-10546. doi:10.1073/pnas.0802008105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10541-10546
    • Carlton, J.G.1    Agromayor, M.2    Martin-Serrano, J.3
  • 10
    • 77958056544 scopus 로고    scopus 로고
    • Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly
    • doi:10.1091/mbc.E10-06-0512
    • Davies, B.A., I.F. Azmi, J. Payne, A. Shestakova, B.F. Horazdovsky, M. Babst, and D.J. Katzmann. 2010. Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly. Mol. Biol. Cell. 21:3396-3408. doi:10.1091/mbc.E10-06-0512
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3396-3408
    • Davies, B.A.1    Azmi, I.F.2    Payne, J.3    Shestakova, A.4    Horazdovsky, B.F.5    Babst, M.6    Katzmann, D.J.7
  • 11
    • 39449086176 scopus 로고    scopus 로고
    • Ist1 regulates Vps4 localization and assembly
    • doi:10.1091/mbc.E07-080-747
    • Dimaano, C., C.B. Jones, A. Hanono, M. Curtiss, and M. Babst. 2008. Ist1 regulates Vps4 localization and assembly. Mol. Biol. Cell. 19:465-474. doi:10.1091/mbc.E07-080-747
    • (2008) Mol. Biol. Cell , vol.19 , pp. 465-474
    • Dimaano, C.1    Jones, C.B.2    Hanono, A.3    Curtiss, M.4    Babst, M.5
  • 12
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: Crucial role of Doa4p ubiquitin isopeptidase
    • doi:10.1128/MCB.21.14.44824494.2001
    • Dupré, S., and R. Haguenauer-Tsapis. 2001. Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase. Mol. Cell. Biol. 21:4482-4494. doi:10.1128/MCB.21.14.44824494.2001
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4482-4494
    • Dupré, S.1    Haguenauer-Tsapis, R.2
  • 13
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • doi:10.1016/j.cell.2007.01.035
    • Fisher, R.D., H.Y. Chung, Q. Zhai, H. Robinson, W.I. Sundquist, and C.P. Hill. 2007. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell. 128:841-852. doi:10.1016/j.cell.2007.01.035
    • (2007) Cell , vol.128 , pp. 841-852
    • Fisher, R.D.1    Chung, H.Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 15
    • 0032546925 scopus 로고    scopus 로고
    • The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner
    • doi:10.1074/jbc.273.25.15818
    • Gerhardt, B., T.J. Kordas, C.M. Thompson, P. Patel, and T. Vida. 1998. The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner. J. Biol. Chem. 273:15818-15829. doi:10.1074/jbc.273.25.15818
    • (1998) J. Biol. Chem. , vol.273 , pp. 15818-15829
    • Gerhardt, B.1    Kordas, T.J.2    Thompson, C.M.3    Patel, P.4    Vida, T.5
  • 16
    • 68449095867 scopus 로고    scopus 로고
    • Structure and function of the ESCRT-IIIII interface in multivesicular body biogenesis
    • doi:10.1016/j.devcel.2009.07.008
    • Im, Y.J., T. Wollert, E. Boura, and J.H. Hurley. 2009. Structure and function of the ESCRT-IIIII interface in multivesicular body biogenesis. Dev. Cell. 17:234-243. doi:10.1016/j.devcel.2009.07.008
    • (2009) Dev. Cell , vol.17 , pp. 234-243
    • Im, Y.J.1    Wollert, T.2    Boura, E.3    Hurley, J.H.4
  • 17
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • doi:10.1016/S0092-8674(01)00434-2
    • Katzmann, D.J., M. Babst, and S.D. Emr. 2001. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:145-155. doi:10.1016/S0092-8674(01)00434-2
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 18
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • doi:10.1083/jcb.200302136
    • Katzmann, D.J., C.J. Stefan, M. Babst, and S.D. Emr. 2003. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162:413-423. doi:10.1083/jcb.200302136
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 19
    • 46049099346 scopus 로고    scopus 로고
    • Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding
    • doi:10.1016/j.devcel.2008.05.014
    • Kieffer, C., J.J. Skalicky, E. Morita, I. De Domenico, D.M. Ward, J. Kaplan, and W.I. Sundquist. 2008. Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding. Dev. Cell. 15:62-73. doi:10.1016/j.devcel.2008.05.014
    • (2008) Dev. Cell , vol.15 , pp. 62-73
    • Kieffer, C.1    Skalicky, J.J.2    Morita, E.3    De Domenico, I.4    Ward, D.M.5    Kaplan, J.6    Sundquist, W.I.7
  • 20
    • 19944375126 scopus 로고    scopus 로고
    • Structural basis for endosomal targeting by the Bro1 domain
    • doi:10.1016/j.devcel.2005.04.001
    • Kim, J., S. Sitaraman, A. Hierro, B.M. Beach, G. Odorizzi, and J.H. Hurley. 2005. Structural basis for endosomal targeting by the Bro1 domain. Dev. Cell. 8:937-947. doi:10.1016/j.devcel.2005.04.001
    • (2005) Dev. Cell , vol.8 , pp. 937-947
    • Kim, J.1    Sitaraman, S.2    Hierro, A.3    Beach, B.M.4    Odorizzi, G.5    Hurley, J.H.6
  • 22
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • doi:10.1002/(SICI)1097-0061(199807)14:10〈953::AID-YEA293〉3.0. CO;2-U
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961. doi:10.1002/(SICI)1097-0061(199807)14: 10〈953::AID-YEA293〉3.0.CO;2-U
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 23
    • 0035173239 scopus 로고    scopus 로고
    • Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 Mutant
    • Losko, S., F. Kopp, A. Kranz, and R. Kölling. 2001. Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 Mutant. Mol. Biol. Cell. 12:1047-1059.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1047-1059
    • Losko, S.1    Kopp, F.2    Kranz, A.3    Kölling, R.4
  • 24
    • 4444342179 scopus 로고    scopus 로고
    • Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes
    • doi:10.1083/jcb.200403139
    • Luhtala, N., and G. Odorizzi. 2004. Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes. J. Cell Biol. 166:717-729. doi:10.1083/jcb.200403139
    • (2004) J. Cell Biol. , vol.166 , pp. 717-729
    • Luhtala, N.1    Odorizzi, G.2
  • 25
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • doi:10.1038/nm1201-1313
    • Martin-Serrano, J., T. Zang, and P.D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319. doi:10.1038/nm1201-1313
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 27
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRT machinery in viral budding and cytokinesis
    • doi:10.1242/jcs.028308
    • McDonald, B., and J. Martin-Serrano. 2009. No strings attached: the ESCRT machinery in viral budding and cytokinesis. J. Cell Sci. 122:2167-2177. doi:10.1242/jcs.028308
    • (2009) J. Cell Sci. , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 28
    • 34347339528 scopus 로고    scopus 로고
    • Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding
    • doi:10.1016/j.chom.2007.06.003
    • Morita, E., V. Sandrin, S.L. Alam, D.M. Eckert, S.P. Gygi, and W.I. Sundquist. 2007. Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding. Cell Host Microbe. 2:41-53. doi:10.1016/j.chom.2007. 06.003
    • (2007) Cell Host Microbe. , vol.2 , pp. 41-53
    • Morita, E.1    Sandrin, V.2    Alam, S.L.3    Eckert, D.M.4    Gygi, S.P.5    Sundquist, W.I.6
  • 29
    • 33845317263 scopus 로고    scopus 로고
    • Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes
    • doi:10.1083/jcb.200606113
    • Nickerson, D.P., M. West, and G. Odorizzi. 2006. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J. Cell Biol. 175:715-720. doi:10.1083/jcb.200606113
    • (2006) J. Cell Biol. , vol.175 , pp. 715-720
    • Nickerson, D.P.1    West, M.2    Odorizzi, G.3
  • 30
    • 77949465181 scopus 로고    scopus 로고
    • Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles
    • doi:10.1091/mbc.E09-09-0776
    • Nickerson, D.P., M. West, R. Henry, and G. Odorizzi. 2010. Regulators of Vps4 ATPase activity at endosomes differentially influence the size and rate of formation of intralumenal vesicles. Mol. Biol. Cell. 21:1023-1032. doi:10.1091/mbc.E09-09-0776
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1023-1032
    • Nickerson, D.P.1    West, M.2    Henry, R.3    Odorizzi, G.4
  • 31
    • 35148831808 scopus 로고    scopus 로고
    • Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
    • doi:10.1038/nature06171
    • Obita, T., S. Saksena, S. Ghazi-Tabatabai, D.J. Gill, O. Perisic, S.D. Emr, and R.L. Williams. 2007. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature. 449:735-739. doi:10.1038/nature06171
    • (2007) Nature , vol.449 , pp. 735-739
    • Obita, T.1    Saksena, S.2    Ghazi-Tabatabai, S.3    Gill, D.J.4    Perisic, O.5    Emr, S.D.6    Williams, R.L.7
  • 32
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • doi:10.1016/S0092-8674(00)81707-9
    • Odorizzi, G., M. Babst, and S.D. Emr. 1998. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell. 95:847-858. doi:10.1016/S0092-8674(00)81707-9
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 33
    • 0038784064 scopus 로고    scopus 로고
    • Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae
    • doi:10.1242/jcs.00395
    • Odorizzi, G., D.J. Katzmann, M. Babst, A. Audhya, and S.D. Emr. 2003. Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae. J. Cell Sci. 116:1893-1903. doi:10.1242/jcs.00395
    • (2003) J. Cell Sci. , vol.116 , pp. 1893-1903
    • Odorizzi, G.1    Katzmann, D.J.2    Babst, M.3    Audhya, A.4    Emr, S.D.5
  • 34
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • doi:10.1146/annurev.cellbio.23.090506.123319
    • Piper, R.C., and D.J. Katzmann. 2007. Biogenesis and function of multivesicular bodies. Annu. Rev. Cell Dev. Biol. 23:519-547. doi:10.1146/annurev.cellbio.23.090506.123319
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 35
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • doi:10.1038/nature07961
    • Raiborg, C., and H. Stenmark. 2009. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature. 458:445-452. doi:10.1038/nature07961
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 36
    • 34249073136 scopus 로고    scopus 로고
    • Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies
    • doi:10.1038/sj.emboj.7601692
    • Richter, C., M. West, and G. Odorizzi. 2007. Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies. EMBO J. 26:2454-2464. doi:10.1038/sj.emboj.7601692
    • (2007) EMBO J. , vol.26 , pp. 2454-2464
    • Richter, C.1    West, M.2    Odorizzi, G.3
  • 37
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder, S.E., L.M. Banta, K. Köhrer, J.M. McCaffery, and S.D. Emr. 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    Köhrer, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 38
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., D.J. Klionsky, L.M. Banta, and S.D. Emr. 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
  • 39
    • 35648973707 scopus 로고    scopus 로고
    • The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation
    • doi:10.1074/jbc.M704009200
    • Row, P.E., H. Liu, S. Hayes, R. Welchman, P. Charalabous, K. Hofmann, M.J. Clague, C.M. Sanderson, and S. Urbé. 2007. The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation. J. Biol. Chem. 282:30929-30937. doi:10.1074/jbc.M704009200
    • (2007) J. Biol. Chem. , vol.282 , pp. 30929-30937
    • Row, P.E.1    Liu, H.2    Hayes, S.3    Welchman, R.4    Charalabous, P.5    Hofmann, K.6    Clague, M.J.7    Sanderson, C.M.8    Urbé, S.9
  • 40
    • 39449140052 scopus 로고    scopus 로고
    • Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting
    • doi:10.1091/mbc.E07070694
    • Rue, S.M., S. Mattei, S. Saksena, and S.D. Emr. 2008. Novel Ist1-Did2 complex functions at a late step in multivesicular body sorting. Mol. Biol. Cell. 19:475-484. doi:10.1091/mbc.E07070694
    • (2008) Mol. Biol. Cell , vol.19 , pp. 475-484
    • Rue, S.M.1    Mattei, S.2    Saksena, S.3    Emr, S.D.4
  • 41
    • 2342423251 scopus 로고    scopus 로고
    • ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
    • doi:10.1242/jcs.00998
    • Sachse, M., G.J. Strous, and J. Klumperman. 2004. ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell Sci. 117:1699-1708. doi:10.1242/jcs.00998
    • (2004) J. Cell Sci. , vol.117 , pp. 1699-1708
    • Sachse, M.1    Strous, G.J.2    Klumperman, J.3
  • 42
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • doi:10.1016/j.cell.2008.11.013
    • Saksena, S., J. Wahlman, D. Teis, A.E. Johnson, and S.D. Emr. 2009. Functional reconstitution of ESCRT-III assembly and disassembly. Cell. 136:97-109. doi:10.1016/j.cell.2008.11.013
    • (2009) Cell , vol.136 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 44
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • doi:10.1016/S0092-8674(03)00653-6
    • Strack, B., A. Calistri, S. Craig, E. Popova, and H.G. Göttlinger. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell. 114:689-699. doi:10.1016/S0092-8674(03)00653-6
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Göttlinger, H.G.5
  • 46
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • doi:10.1006/prep.2000.1363
    • Tan, S. 2001. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli. Protein Expr. Purif. 21:224-234. doi:10.1006/prep.2000.1363
    • (2001) Protein Expr. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 47
    • 53249131094 scopus 로고    scopus 로고
    • Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation
    • doi:10.1016/j.devcel.2008.08.013
    • Teis, D., S. Saksena, and S.D. Emr. 2008. Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Dev. Cell. 15:578-589. doi:10.1016/j.devcel.2008.08.013
    • (2008) Dev. Cell , vol.15 , pp. 578-589
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 48
    • 5044245523 scopus 로고    scopus 로고
    • ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes
    • doi:10.1016/j.devcel.2004.09.003
    • Teo, H., O. Perisic, B. González, and R.L. Williams. 2004. ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. Dev. Cell. 7:559-569. doi:10.1016/j.devcel.2004.09.003
    • (2004) Dev. Cell , vol.7 , pp. 559-569
    • Teo, H.1    Perisic, O.2    González, B.3    Williams, R.L.4
  • 49
    • 33747795207 scopus 로고    scopus 로고
    • A systematic analysis of human CHMP protein interactions: Additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex
    • doi:10.1016/j.ygeno.2006.04.003
    • Tsang, H.T., J.W. Connell, S.E. Brown, A. Thompson, E. Reid, and C.M. Sanderson. 2006. A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. Genomics. 88:333-346. doi:10.1016/j.ygeno.2006.04.003
    • (2006) Genomics , vol.88 , pp. 333-346
    • Tsang, H.T.1    Connell, J.W.2    Brown, S.E.3    Thompson, A.4    Reid, E.5    Sanderson, C.M.6
  • 50
    • 34249943479 scopus 로고    scopus 로고
    • Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site
    • doi:10.1128/JVI.00314-07
    • Usami, Y., S. Popov, and H.G. Göttlinger. 2007. Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site. J. Virol. 81:6614-6622. doi:10.1128/JVI.00314-07
    • (2007) J. Virol. , vol.81 , pp. 6614-6622
    • Usami, Y.1    Popov, S.2    Göttlinger, H.G.3
  • 51
    • 0034940214 scopus 로고    scopus 로고
    • Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)
    • doi:10.1073/pnas.131059198
    • VerPlank, L., F. Bouamr, T.J. LaGrassa, B. Agresta, A. Kikonyogo, J. Leis, and C.A. Carter. 2001. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc. Natl. Acad. Sci. USA. 98:7724-7729. doi:10.1073/pnas.131059198
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7724-7729
    • VerPlank, L.1    Bouamr, F.2    LaGrassa, T.J.3    Agresta, B.4    Kikonyogo, A.5    Leis, J.6    Carter, C.A.7
  • 52
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert, T., and J.H. Hurley. 2010. Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature. 464:864-869.
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2


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