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Volumn 88, Issue 3, 2006, Pages 333-346

A systematic analysis of human CHMP protein interactions: Additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex

Author keywords

CHMP; ESCRT III complex; MIT domain; Multivesicular bodies; Protein complementation assay; Protein interaction network; Yeast two hybrid

Indexed keywords

CHMP PROTEIN; ENDOSOMAL SORTING COMPLEX REQUIRED FOR TRANSPORT III COMPLEX; MICROTUBULE INTERACTING AND TRANSPORT DOMAIN CONTAINING PROTEIN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33747795207     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2006.04.003     Document Type: Article
Times cited : (134)

References (36)
  • 1
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski J.L., and 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
  • 2
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1
    • Katzmann D.J., Babst M., and Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1. Cell 106 (2001) 145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 3
    • 0035903635 scopus 로고    scopus 로고
    • Sorting of proteins into multivesicular bodies: ubiquitin-dependent and independent targeting
    • Reggiori F., and Pelham H.R. 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.2
  • 4
    • 0033767690 scopus 로고    scopus 로고
    • Exosome: from internal vesicle of the multivesicular body to intercellular signaling device
    • Denzer K., Kleijmeer M.J., Heijnen H.F., Stoorvogel W., and Geuze H.J. Exosome: from internal vesicle of the multivesicular body to intercellular signaling device. J. Cell Sci. 113 (2000) 3365
    • (2000) J. Cell Sci. , vol.113 , pp. 3365
    • Denzer, K.1    Kleijmeer, M.J.2    Heijnen, H.F.3    Stoorvogel, W.4    Geuze, H.J.5
  • 5
    • 0029989258 scopus 로고    scopus 로고
    • B lymphocytes secrete antigen-presenting vesicles
    • Raposo G., et al. B lymphocytes secrete antigen-presenting vesicles. J. Exp. Med. 183 (1996) 1
    • (1996) J. Exp. Med. , vol.183 , pp. 1
    • Raposo, G.1
  • 6
    • 0036418964 scopus 로고    scopus 로고
    • The plasticity of multivesicular bodies and the regulation of antigen presentation
    • Murk J.-L., Stoorvogel W., Kleijmeer M.J., and Geuze H.J. The plasticity of multivesicular bodies and the regulation of antigen presentation. Cell Dev. Biol. 13 (2002) 303-311
    • (2002) Cell Dev. Biol. , vol.13 , pp. 303-311
    • Murk, J.-L.1    Stoorvogel, W.2    Kleijmeer, M.J.3    Geuze, H.J.4
  • 7
    • 0036788110 scopus 로고    scopus 로고
    • Human macrophages accumulate HIV-1 particles in MHC II compartments
    • Raposo G., et al. Human macrophages accumulate HIV-1 particles in MHC II compartments. Traffic 3 (2002) 718-729
    • (2002) Traffic , vol.3 , pp. 718-729
    • Raposo, G.1
  • 8
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews A., et al. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162 (2003) 443-455
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1
  • 9
    • 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., and 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
  • 10
    • 10744233294 scopus 로고    scopus 로고
    • The protein network of HIV budding
    • von Schwedler U.K., et al. The protein network of HIV budding. Cell 114 (2003) 701-713
    • (2003) Cell , vol.114 , pp. 701-713
    • von Schwedler, U.K.1
  • 11
    • 0032516807 scopus 로고    scopus 로고
    • Multiple sorting pathways between the late Golgi and the vacuole in yeast
    • Conibear E., and Stevens T.H. Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim. Biophys. Acta 1404 (1998) 211-230
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 211-230
    • Conibear, E.1    Stevens, T.H.2
  • 12
    • 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. Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol. Biol. Cell 7 (1996) 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
  • 13
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumour susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M., Odorizzi G., Estepa E.J., and Emr S.D. Mammalian tumour 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
  • 14
    • 1642373357 scopus 로고    scopus 로고
    • Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae
    • Bowers K., et al. Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic 5 (2004) 194-210
    • (2004) Traffic , vol.5 , pp. 194-210
    • Bowers, K.1
  • 15
    • 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., and 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
  • 16
    • 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., and 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
  • 17
    • 0035172587 scopus 로고    scopus 로고
    • A family of small coiled-coil-forming proteins functioning at the late endosome in yeast
    • Kranz A., and Kinner R. A family of small coiled-coil-forming proteins functioning at the late endosome in yeast. Mol. Biol. Cell 12 (2001) 711-723
    • (2001) Mol. Biol. Cell , vol.12 , pp. 711-723
    • Kranz, A.1    Kinner, R.2
  • 18
    • 12444278931 scopus 로고    scopus 로고
    • Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
    • Yeo S.C., et al. Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae. J. Cell Sci. 116 (2003) 3957-3970
    • (2003) J. Cell Sci. , vol.116 , pp. 3957-3970
    • Yeo, S.C.1
  • 19
    • 0034926390 scopus 로고    scopus 로고
    • CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins
    • Howard T.L., Stauffer D.R., Degnin C.R., and Hollenberg S.M. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J. Cell Sci. 114 (2001) 2395-2404
    • (2001) J. Cell Sci. , vol.114 , pp. 2395-2404
    • Howard, T.L.1    Stauffer, D.R.2    Degnin, C.R.3    Hollenberg, S.M.4
  • 20
    • 0034916615 scopus 로고    scopus 로고
    • CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression
    • Stauffer D.R., Howard T.L., Nyun T., and Hollenberg S.M. CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression. J. Cell Sci. 114 (2001) 2383-2393
    • (2001) J. Cell Sci. , vol.114 , pp. 2383-2393
    • Stauffer, D.R.1    Howard, T.L.2    Nyun, T.3    Hollenberg, S.M.4
  • 21
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and host strain designed for high efficient two-hybrid selection in yeast
    • James P., and Halladay J. Genomic libraries and host strain designed for high efficient two-hybrid selection in yeast. Genomics 144 (1996) 1425-1436
    • (1996) Genomics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2
  • 22
    • 0344688165 scopus 로고    scopus 로고
    • Analysis of a high throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region
    • Lehner B., et al. Analysis of a high throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. Genomics 83 (2004) 153-167
    • (2004) Genomics , vol.83 , pp. 153-167
    • Lehner, B.1
  • 23
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome scale map of the human protein-protein interaction network
    • Rual J.F., et al. Towards a proteome scale map of the human protein-protein interaction network. Nature 437 (2005) 1173-1178
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1
  • 24
    • 22144460159 scopus 로고    scopus 로고
    • Structural characterization of the MIT domain from human Vps4b
    • Takasu H., et al. Structural characterization of the MIT domain from human Vps4b. Biochem. Biophys. Res. Commun. 334 (2005) 460-465
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 460-465
    • Takasu, H.1
  • 25
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • Reid E., et al. The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum. Mol. Genet. 14 (2005) 19-38
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 19-38
    • Reid, E.1
  • 26
    • 25444442371 scopus 로고    scopus 로고
    • Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A
    • Scott A., et al. Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A. Proc. Natl. Acad. Sci. USA 102 (2005) 13813-13818
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13813-13818
    • Scott, A.1
  • 27
    • 27144444327 scopus 로고    scopus 로고
    • Structural and mechanistic studies of VPS4 proteins
    • Scott A., et al. Structural and mechanistic studies of VPS4 proteins. EMBO J. 24 (2005) 3658-3669
    • (2005) EMBO J. , vol.24 , pp. 3658-3669
    • Scott, A.1
  • 28
    • 0345600247 scopus 로고    scopus 로고
    • A protein interaction map of Drosophila melanogaster
    • Giot L., et al. A protein interaction map of Drosophila melanogaster. Science 302 (2003) 1727-1736
    • (2003) Science , vol.302 , pp. 1727-1736
    • Giot, L.1
  • 29
    • 0035984722 scopus 로고    scopus 로고
    • β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau A., Primeau M., Trueau L.-E., and Michnick S.W. β-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol. 20 (2002) 619-622
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trueau, L.-E.3    Michnick, S.W.4
  • 30
    • 0037133629 scopus 로고    scopus 로고
    • Protein-protein interactions monitored in mammalian cells via complementation of beta-lactamase enzyme fragments
    • Wehrman T., Kleaveland B., Her J.H., Balint R.F., and Blau H.M. Protein-protein interactions monitored in mammalian cells via complementation of beta-lactamase enzyme fragments. Proc. Natl. Acad. Sci. USA 99 (2002) 3469-3474
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3469-3474
    • Wehrman, T.1    Kleaveland, B.2    Her, J.H.3    Balint, R.F.4    Blau, H.M.5
  • 31
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • Lehner B., and Sanderson C.M. A protein interaction framework for human mRNA degradation. Genome Res. 14 (2004) 1315-1323
    • (2004) Genome Res. , vol.14 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 32
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough J., Clague M.J., and Urbé S. AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell. Biol. 166 (2004) 487-492
    • (2004) J. Cell. Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbé, S.3
  • 33
    • 1342325811 scopus 로고    scopus 로고
    • Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe
    • Onishi M., Nakamura Y., Koga T., Takegawa K., and Fukui Y. Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe. Biosci. Biotechnol. Biochem. 67 (2003) 1772-1779
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1772-1779
    • Onishi, M.1    Nakamura, Y.2    Koga, T.3    Takegawa, K.4    Fukui, Y.5
  • 34
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • McCullough J., et al. Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 16 (2006) 160-165
    • (2006) Curr. Biol. , vol.16 , pp. 160-165
    • McCullough, J.1
  • 35
    • 15444369744 scopus 로고    scopus 로고
    • The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells
    • Ward D.M., et al. The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells. J. Biol. Chem. 280 (2005) 10548-10555
    • (2005) J. Biol. Chem. , vol.280 , pp. 10548-10555
    • Ward, D.M.1
  • 36
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endosomal degradation of class I molecules
    • Duncan L.M., et al. Lysine-63-linked ubiquitination is required for endosomal degradation of class I molecules. EMBO J. 25 (2006) 1635-1645
    • (2006) EMBO J. , vol.25 , pp. 1635-1645
    • Duncan, L.M.1


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