메뉴 건너뛰기




Volumn 400, Issue 1, 2006, Pages 23-32

CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway

Author keywords

Changed multivesicular body protein (CHMP); Endosomal sorting complex required for transport (ESCRT); Multivesicular body; Retrovirus; SNF7

Indexed keywords

AMINO ACIDS; BIOASSAY; CELLS; MICROSCOPIC EXAMINATION; SORTING; VIRUSES; YEAST;

EID: 33751092256     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060897     Document Type: Article
Times cited : (57)

References (42)
  • 1
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., Odorizzi, G. and Emr, S. D. (2002) Receptor downregulation and multivesicular-body sorting. Nat. Rev. Mol. Cell Biol. 3, 893-905
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 2
  • 3
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst, M. (2005) A protein's final ESCRT. Traffic 6, 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 4
    • 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
  • 5
    • 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. (2002) Escrt-III: an endosome-associated heterooligomeric protein complex required for MVB sorting. Dev. Cell 3, 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
  • 6
    • 0033786796 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
    • Amerik, A. Y., Nowak, J., Swaminathan, S. and Hochstrasser, M. (2000) The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365-3380
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3365-3380
    • Amerik, A.Y.1    Nowak, J.2    Swaminathan, S.3    Hochstrasser, M.4
  • 7
    • 0035172587 scopus 로고    scopus 로고
    • A family of small coiled-coil-forming proteins functioning at the late endosome in yeast
    • Kranz, A., Kinner, A. and Kolling, R. (2001) A family of small coiled-coil-forming proteins functioning at the late endosome in yeast. Mol. Biol. Cell 12, 711-723
    • (2001) Mol. Biol. Cell , vol.12 , pp. 711-723
    • Kranz, A.1    Kinner, A.2    Kolling, R.3
  • 8
    • 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. (2001) CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J. Cell Sci. 114, 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
  • 9
    • 0141643096 scopus 로고    scopus 로고
    • The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
    • Katoh, K., Shibata, H., Suzuki, H., Nara, A., Ishidoh, K., Kominami, E., Yoshimori, T. and Maki, M. (2003) The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J. Biol. Chem. 278, 39104-39113
    • (2003) J. Biol. Chem. , vol.278 , pp. 39104-39113
    • Katoh, K.1    Shibata, H.2    Suzuki, H.3    Nara, A.4    Ishidoh, K.5    Kominami, E.6    Yoshimori, T.7    Maki, M.8
  • 10
    • 0346848903 scopus 로고    scopus 로고
    • CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms
    • Katoh, K., Shibata, H., Hatta, K. and Maki, M. (2004) CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms. Arch. Biochem. Biophys. 421, 159-165
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 159-165
    • Katoh, K.1    Shibata, H.2    Hatta, K.3    Maki, M.4
  • 12
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., Calistri, A., Craig, S., Popova, E. and Gottlinger, H. G. (2003) AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114, 689-699
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 13
    • 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. (2003) Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. U.S.A. 100, 12414-12419
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 14
    • 17144377439 scopus 로고    scopus 로고
    • Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting
    • Yorikawa, C., Shibata, H., Waguri, S., Hatta, K., Horii, M., Katoh, K., Kobayashi, T., Uchiyama, Y. and Maki, M. (2005) Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting. Biochem J. 387, 17-26
    • (2005) Biochem J. , vol.387 , pp. 17-26
    • Yorikawa, C.1    Shibata, H.2    Waguri, S.3    Hatta, K.4    Horii, M.5    Katoh, K.6    Kobayashi, T.7    Uchiyama, Y.8    Maki, M.9
  • 16
    • 1242314744 scopus 로고    scopus 로고
    • Structure and function of human Vps20 and Snf7 proteins
    • Peck, J. W., Bowden, E. T. and Burbelo, P. D. (2004) Structure and function of human Vps20 and Snf7 proteins. Biochem. J. 377, 693-700
    • (2004) Biochem. J. , vol.377 , pp. 693-700
    • Peck, J.W.1    Bowden, E.T.2    Burbelo, P.D.3
  • 17
    • 12344250580 scopus 로고    scopus 로고
    • The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B
    • Reid, E., Connell, J., Edwards, T. L., Duley, S., Brown, S. E. and Sanderson, C. M. (2005) The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B. Hum. Mol. Genet. 14, 19-38
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 19-38
    • Reid, E.1    Connell, J.2    Edwards, T.L.3    Duley, S.4    Brown, S.E.5    Sanderson, C.M.6
  • 19
    • 33645797370 scopus 로고    scopus 로고
    • Cellular factors required for Lassa virus budding
    • Urata, S., Noda, T., Kawaoka, Y., Yokosawa, H. and Yasuda, J. (2006) Cellular factors required for Lassa virus budding. J. Virol. 80, 4191-4195
    • (2006) J. Virol. , vol.80 , pp. 4191-4195
    • Urata, S.1    Noda, T.2    Kawaoka, Y.3    Yokosawa, H.4    Yasuda, J.5
  • 24
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: An efficient and stable system lor transient packaging of retroviruses
    • Morita, S., Kojima, T. and Kitamura, T. (2000) Plat-E: an efficient and stable system lor transient packaging of retroviruses. Gene Ther. 7, 1063-1066
    • (2000) Gene Ther. , vol.7 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 25
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., Wendland, B., Estepa, E. J. and Emr, S. D. (1998) The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 26
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop, N. and Woodman, P. (2000) ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell 11, 227-239
    • (2000) Mol. Biol. Cell , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 27
    • 0037439880 scopus 로고    scopus 로고
    • A dominant negative form of the AAA ATPase SKD1/VPS4 impairs membrane trafficking out of endosomal/lysosomal compartments: Class E vps phenotype in mammalian cells
    • Fujita, H., Yamanaka, M., Imamura, K., Tanaka, Y., Nara, A., Yoshimori, T., Yokota, S. and Himeno, M. (2003) A dominant negative form of the AAA ATPase SKD1/VPS4 impairs membrane trafficking out of endosomal/lysosomal compartments: class E vps phenotype in mammalian cells. J. Cell Sci. 116, 401-414
    • (2003) J. Cell Sci. , vol.116 , pp. 401-414
    • Fujita, H.1    Yamanaka, M.2    Imamura, K.3    Tanaka, Y.4    Nara, A.5    Yoshimori, T.6    Yokota, S.7    Himeno, M.8
  • 29
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund, K., Di Fiore, P. P. and Dikic, I. (2003) Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28, 598-603
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 30
    • 0035545823 scopus 로고    scopus 로고
    • Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues
    • Usuba, T., Ishibashi, Y., Okawa, Y., Hirakawa, T., Takada, K. and Ohkawa, K. (2001) Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues. Int. J. Cancer 94, 662-668
    • (2001) Int. J. Cancer , vol.94 , pp. 662-668
    • Usuba, T.1    Ishibashi, Y.2    Okawa, Y.3    Hirakawa, T.4    Takada, K.5    Ohkawa, K.6
  • 31
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P. and Dikic, I. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5, 461-466
    • (2003) Nat. Cell Biol. , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 33
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov, D. G. and Freed, E. O. (2004) Retrovirus budding. Virus Res. 106, 87-102
    • (2004) Virus Res. , vol.106 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 34
    • 22844435415 scopus 로고    scopus 로고
    • Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding
    • Segura-Morales, C., Pescia, C., Chatellard-Causse, C., Sadoul, R., Bertrand, E. and Basyuk, E. (2005) Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding. J. Biol. Chem. 288, 27004-27012
    • (2005) J. Biol. Chem. , vol.288 , pp. 27004-27012
    • Segura-Morales, C.1    Pescia, C.2    Chatellard-Causse, C.3    Sadoul, R.4    Bertrand, E.5    Basyuk, E.6
  • 35
    • 23144434990 scopus 로고    scopus 로고
    • Intracellular trafficking of HIV-1 Gag: How Gag interacts with cell membranes and makes viral particles
    • Resh, M. D. (2005) Intracellular trafficking of HIV-1 Gag: how Gag interacts with cell membranes and makes viral particles. AIDS Rev. 7, 84-91
    • (2005) AIDS Rev. , vol.7 , pp. 84-91
    • Resh, M.D.1
  • 37
  • 38
    • 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
    • Tsang, H. T., Cornell, J. W., Brown, S. E., Thompson, A., Reid, E. and Sanderson, C. M. (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
    • (2006) Genomics , vol.88 , pp. 333-346
    • Tsang, H.T.1    Cornell, J.W.2    Brown, S.E.3    Thompson, A.4    Reid, E.5    Sanderson, C.M.6
  • 39
    • 5044245523 scopus 로고    scopus 로고
    • ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes
    • Teo, H., Perisic, O., Gonzalez, B. and Williams, R. L. (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
    • (2004) Dev. Cell , vol.7 , pp. 559-569
    • Teo, H.1    Perisic, O.2    Gonzalez, B.3    Williams, R.L.4
  • 40
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII
    • Bowers, K., Piper, S. C., Edeling, M. A., Gray, S. R., Owen, D. J., Lehner, P. J. and Luzio, J. P. (2006) Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J. Biol. Chem. 281, 5094-5105
    • (2006) J. Biol. Chem. , vol.281 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 41
    • 33745761343 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment
    • Pineda-Molina, E., Belrhali, H., Piefer, A. J., Akula, I., Bates, P. and Weissenhorn, W. (2006) The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Traffic 7, 1007-1016
    • (2006) Traffic , vol.7 , pp. 1007-1016
    • Pineda-Molina, E.1    Belrhali, H.2    Piefer, A.J.3    Akula, I.4    Bates, P.5    Weissenhorn, W.6
  • 42
    • 0037138403 scopus 로고    scopus 로고
    • Calmodulin signaling via the IQ motif
    • Bähler, M. and Rhoads, A. (2002) Calmodulin signaling via the IQ motif. FEBS Lett. 20, 107-113
    • (2002) FEBS Lett. , vol.20 , pp. 107-113
    • Bähler, M.1    Rhoads, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.