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Volumn 7, Issue 4, 2004, Pages 559-569

ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN SUBUNIT;

EID: 5044245523     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2004.09.003     Document Type: Article
Times cited : (185)

References (47)
  • 2
    • 0032476052 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase
    • Ashrafi K. Farazi T.A. Gordon J.I. A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase J. Biol. Chem. 273 1998 25864-25874
    • (1998) J. Biol. Chem. , vol.273 , pp. 25864-25874
    • Ashrafi, K.1    Farazi, T.A.2    Gordon, J.I.3
  • 3
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M. Odorizzi G. Estepa E.J. Emr S.D. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking Traffic 1 2000 248-258
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 4
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M. Katzmann D.J. Estepa-Sabal E.J. Meerloo T. Emr S.D. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting Dev. Cell 3 2002 271-282
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 5
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst M. Katzmann D.J. Snyder W.B. Wendland B. Emr S.D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body Dev. Cell 3 2002 283-289
    • (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
  • 6
    • 4344570298 scopus 로고    scopus 로고
    • The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor downregulation
    • Bache K.G. Slagsvold T. Cabezas A. Rosendal K.R. Raiborg C. Stenmark H. The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor downregulation Mol. Biol. Cell 15 2004 4337-4346
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4337-4346
    • Bache, K.G.1    Slagsvold, T.2    Cabezas, A.3    Rosendal, K.R.4    Raiborg, C.5    Stenmark, H.6
  • 7
    • 0035853688 scopus 로고    scopus 로고
    • TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes
    • Bishop N. Woodman P. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes J. Biol. Chem. 276 2001 11735-11742
    • (2001) J. Biol. Chem. , vol.276 , pp. 11735-11742
    • Bishop, N.1    Woodman, P.2
  • 8
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S. Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes Annu. Rev. Biochem. 72 2003 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computing Project 4)
    • CCP4 (Collaborative Computing Project 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50 1994 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 11
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K.L. Halay E.D. Lai E. Burley S.K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5 Nature 364 1993 412-420
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 12
    • 0036672208 scopus 로고    scopus 로고
    • An ESCRT into the endosome
    • Conibear E. An ESCRT into the endosome Mol. Cell 10 2002 215-216
    • (2002) Mol. Cell , vol.10 , pp. 215-216
    • Conibear, E.1
  • 13
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E. Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • de La Fortelle, E.1    Bricogne, G.2
  • 14
    • 0035149694 scopus 로고    scopus 로고
    • Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis
    • Dunn R. Hicke L. Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis Mol. Biol. Cell 12 2001 421-435
    • (2001) Mol. Biol. Cell , vol.12 , pp. 421-435
    • Dunn, R.1    Hicke, L.2
  • 19
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema E.H. Valdez-Taubas J. Pelham H.R. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins EMBO J. 23 2004 1279-1288
    • (2004) EMBO J. , vol.23 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.3
  • 20
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L. Dunn R. Regulation of membrane transport by ubiquitin and ubiquitin-binding proteins Annu. Rev. Cell Dev. Biol. 19 2003 141-172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 21
    • 0034070805 scopus 로고    scopus 로고
    • Optimizing DREAR and SnB parameters for determining Se-atom substructures
    • Howell P.L. Blessing R.H. Smith G.D. Weeks C.M. Optimizing DREAR and SnB parameters for determining Se-atom substructures Acta Crystallogr. D 56 2000 604-617
    • (2000) Acta Crystallogr. D , vol.56 , pp. 604-617
    • Howell, P.L.1    Blessing, R.H.2    Smith, G.D.3    Weeks, C.M.4
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A. Zou J.-Y. Cowan S.W. Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
  • 24
    • 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
    • Katzmann D.J. Babst M. Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I Cell 106 2001 145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 26
    • 0742288063 scopus 로고    scopus 로고
    • Multivesicular body sorting: Ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S
    • Katzmann D.J. Sarkar S. Chu T. Audhya A. Emr S.D. Multivesicular body sorting: ubiquitin ligase Rsp5 is required for the modification and sorting of carboxypeptidase S Mol. Biol. Cell 15 2004 468-480
    • (2004) Mol. Biol. Cell , vol.15 , pp. 468-480
    • Katzmann, D.J.1    Sarkar, S.2    Chu, T.3    Audhya, A.4    Emr, S.D.5
  • 28
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • (Warrington, UK: Daresbury Laboratory)
    • Leslie, A.G.W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. In Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography (Warrington, UK: Daresbury Laboratory).
    • (1992) Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography
    • Leslie, A.G.W.1
  • 29
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • Li L. Cohen S.N. Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells Cell 85 1996 319-329
    • (1996) Cell , vol.85 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 30
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano J. Yarovoy A. Perez-Caballero D. Bieniasz P.D. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins Proc. Natl. Acad. Sci. USA 100 2003 12414-12419
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N. Vagin A.A. Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D 53 1997 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0038386452 scopus 로고    scopus 로고
    • Escape from Cbl-mediated downregulation. A recurrent theme for oncogenic deregulation of receptor tyrosine kinases
    • Peschard P. Park M. Escape from Cbl-mediated downregulation. A recurrent theme for oncogenic deregulation of receptor tyrosine kinases Cancer Cell 3 2003 519-523
    • (2003) Cancer Cell , vol.3 , pp. 519-523
    • Peschard, P.1    Park, M.2
  • 34
    • 0034846497 scopus 로고    scopus 로고
    • Late endosomes: Sorting and partitioning in multivesicular bodies
    • Piper R.C. Luzio J.P. Late endosomes: sorting and partitioning in multivesicular bodies Traffic 2 2001 612-621
    • (2001) Traffic , vol.2 , pp. 612-621
    • Piper, R.C.1    Luzio, J.P.2
  • 37
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: Ubiquitin-dependent and -independent targeting
    • Reggiori F. Pelham H.R.B. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting EMBO J. 20 2001 5176-5186
    • (2001) EMBO J. , vol.20 , pp. 5176-5186
    • Reggiori, F.1    Pelham, H.R.B.2
  • 38
    • 0033618430 scopus 로고    scopus 로고
    • Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II
    • Schmidt A.E. Miller T. Schmidt S.L. Shiekhattar R. Shilatifard A. Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II J. Biol. Chem. 274 1999 21981-21985
    • (1999) J. Biol. Chem. , vol.274 , pp. 21981-21985
    • Schmidt, A.E.1    Miller, T.2    Schmidt, S.L.3    Shiekhattar, R.4    Shilatifard, A.5
  • 43
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • Tan S. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli Protein Expr. Purif. 21 2001 224-234
    • (2001) Protein Expr. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 44
    • 3142581995 scopus 로고    scopus 로고
    • Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins
    • Teo H. Veprintsev D.B. Williams R.L. Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins J. Biol. Chem. 279 2004 28689-28696
    • (2004) J. Biol. Chem. , vol.279 , pp. 28689-28696
    • Teo, H.1    Veprintsev, D.B.2    Williams, R.L.3
  • 45
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski J.L. Piper R.C. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole Traffic 2 2001 622-630
    • (2001) Traffic , vol.2 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 47
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M. Miller R. The design and implementation of SnB v2.0 J. Appl. Crystallogr. 32 1999 120-124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.