The CHMP4b- and Src-docking sites in the Bro1 domain are autoinhibited in the native state of Alix

Biochemical Journal

Volumn 418, Issue 2, 2009, Pages 277-284

  Zhou, Xi ^a   Pan, Shujuan ^a   Sun, Le ^b   Corvera, Joe ^b   Lee, Yu Chen ^a   Lin, Sue Hwa ^a   Kuang, Jian ^a  

^a UNIVERSITY OF TEXAS   (United States)

^b A and G Pharmaceuticals   (United States)

Author keywords

1A3 anti Alix antibody; Apoptosis linked gene 2 interacting protein X (Alix); Bro1 domain; Charged multivesicular body protein 4b (CHMP4b); Human orthologue of Xenopus protein of 95 kDa (Hp95); Src

Indexed keywords

1A3 ANTI-ALIX ANTIBODY; APOPTOSIS-LINKED-GENE-2-INTERACTING PROTEIN X (ALIX); BRO1 DOMAIN; CHARGED MULTIVESICULAR BODY PROTEIN 4B (CHMP4B); HUMAN ORTHOLOGUE OF XENOPUS PROTEIN OF 95 KDA (HP95); SRC;

AMINO ACIDS; ANTIBODIES; CELL DEATH; CELL MEMBRANES; CRYSTALLOGRAPHY; SOAPS (DETERGENTS);

DOCKING;

ADAPTOR PROTEIN; APOPTOSIS LINKED GENE 2 INTERACTING PROTEIN X; BINDING PROTEIN; BRO1 DOMAIN PROTEIN; CHARGED MULTIVESICULAR BODY PROTEIN 4B; CYTOPLASM PROTEIN; EPITOPE; GLUTATHIONE TRANSFERASE; MONOCLONAL ANTIBODY; PROTEIN PATCHED 1; PROTEIN PATCHED 2; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; CARRIER PROTEIN; CELL CYCLE PROTEIN; CHMP4B PROTEIN, HUMAN; PDCD6IP PROTEIN, HUMAN; PHOSPHOPROTEIN; XENOPUS PROTEIN; XP95 PROTEIN, XENOPUS;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL LYSATE; CELL MEMBRANE; CONTROLLED STUDY; CYTOSOL; EMBRYO; ENDOSOME; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SEQUENCE ALIGNMENT; AMINO ACID SEQUENCE; ANIMAL; ANTIBODY COMBINING SITE; BINDING SITE; BIOLOGICAL MODEL; CELL CULTURE; CHEMISTRY; DOWN REGULATION; DRUG ANTAGONISM; HOMEOSTASIS; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; XENOPUS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BINDING SITES, ANTIBODY; CALCIUM-BINDING PROTEINS; CARRIER PROTEINS; CELL CYCLE PROTEINS; CELLS, CULTURED; DOWN-REGULATION; EPITOPES; HOMEOSTASIS; HUMANS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SRC-FAMILY KINASES; XENOPUS; XENOPUS PROTEINS;

EID: 61449173915     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081388     Document Type: Article

References (43)

1. Raiborg, C., Rusten, T. E. and Stenmark, H. (2003) Protein sorting into multivesicular endosomes. Curr. Opin. Cell Biol. 15, 446-455
2. Demirov, D. G. and Freed, E. O. (2004) Retrovirus budding. Virus Res. 106, 87-102
3. Morita, E. and Sundquist, W. I. (2004) Retrovirus budding. Annu. Rev. Cell Dev. Biol. 20, 395-425
4. Babst, M. (2005) A protein's final ESCRT. Traffic 6, 2-9
5. Missotten, M., Nichols, A., Rieger, K. and Sadoul, R. (1999) Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ. 6, 124-129
6. Vito, P., Pellegrini, L., Guiet, C. and D'Adamio, L. (1999) Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction. J. Biol. Chem. 274, 1533-1540
7. Che, S., El-Hodiri, H. M., Wu, C. F., Nelman-Gonzalez, M., Weil, M. M., Etkin, L. D., Clark, R. B. and Kuang, J. (1999) Identification and cloning of xp95, a putative signal transduction protein in Xenopus oocytes. J. Biol. Chem. 274, 5522-5531
8. 1 phase arrest in confluent HeLa cells. Differentiation 67, 139-153
9. Odorizzi, G., Katzmann, D. J., Babst, M., Audhya, A. and Emr, S. D. (2003) Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae. J. Cell Sci. 116, 1893-1903
10. 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
11. von Schwedler, U. K., Stuchell, M., Muller, B., Ward, D. M., Chung, H. Y., Morita, E., Wang, H. E., Davis, T., He, G. P., Cimbora, D. M. et al. (2003) The protein network of HIV budding. Cell 114, 701-713
12. Freed, E. O. and Mouland, A. J. (2006) The cell biology of HIV-1 and other retroviruses. Retrovirology 3, 77
13. Gottlinger, H. G. (2007) How HIV-1 hijacks ALIX. Nat. Struct. Mol. Biol. 14, 254-256
14. Carlton, J. G. and Martin-Serrano, J. (2007) Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery. Science 316, 1908-1912
15. Morita, E., Sandrin, V., Chung, H. Y., Morham, S. G., Gygi, S. P., Rodesch, C. K. and Sundquist, W. I. (2007) Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 26, 4215-4227
16. Mahul-Mellier, A. L., Hemming, F. J., Blot, B., Fraboulet, S. and Sadoul, R. (2006) Alix, making a link between apoptosis-linked gene-2, the endosomal sorting complexes required for transport, and neuronal death in vivo. J. Neurosci. 26, 542-549
17. Sadoul, R. (2006) Do Alix and ALG-2 really control endosomes for better or for worse? Biol. Cell. 98, 69-77
18. Kim, J., Sitaraman, S., Hierro, A., Beach, B. M., Odorizzi, G. and Hurley, J. H. (2005) Structural basis for endosomal targeting by the Bro1 domain. Dev. Cell. 8, 937-947
19. Fisher, R. D., Chung, H. Y., Zhai, Q., Robinson, H., Sundquist, W. I. and Hill, C. P. (2007) Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell 128, 841-852
20. Lee, S., Joshi, A., Nagashima, K., Freed, E. O. and Hurley, J. H. (2007) Structural basis for viral late-domain binding to Alix. Nat. Struct. Mol. Biol. 14, 194-199
21. Dejournett, R. E., Kobayashi, R., Pan, S., Wu, C., Etkin, L. D., Clark, R. B., Bogler, O. and Kuang, J. (2007) Phosphorylation of the proline-rich domain of Xp95 modulates Xp95 interaction with partner proteins. Biochem. J. 401, 521-531
22. Schmidt, M. H., Dikic, I. and Bogler, O. (2005) Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities. J. Biol. Chem. 280, 3414-3425
23. n L late domains of HIV-1 and EIAV. Nat. Struct. Mol. Biol. 15, 43-49
24. Doray, B., Bruns, K., Ghosh, P. and Kornfeld, S. A. (2002) Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc. Natl. Acad. Sci. U.S.A. 99, 8072-8077
25. 2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity. Oncogene 21, 7720-7729
26. Zhou, X., Pan, S., Sun, L., Corvera, J., Lin, S. H. and Kuang, J. (2008) The HIV-1 p6/EIAV p9 docking site in Alix is autoinhibited as revealed by a conformation-sensitive anti-Alix monoclonal antibody. Biochem. J. 414, 215-220
27. 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
28. Zamborlini, A., Usami, Y., Radoshitzky, S. R., Popova, E., Palu, G. and Gottlinger, H. (2006) Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding. Proc. Natl. Acad. Sci. U.S.A. 103, 19140-19145
29. Shim, S., Kimpler, L. A. and Hanson, P. I. (2007) Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 8, 1068-1079
30. Lata, S., Roessle, M., Solomons, J., Jamin, M., Gottlinger, H. G., Svergun, D. I. and Weissenhorn, W. (2008) Structural basis for autoinhibition of ESCRT-III CHMP3. J. Mol. Biol. 378, 816-825
31. 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
32. Bhairi, S. M. and Mohan, C. (2007) Detergents: a Guide to the Properties and Uses of Detergents in Biological Systems, EMD Biosciences, La Jolla
33. Pan, S., Wang, R., Zhou, X., He, G., Koomen, J., Kobayashi, R., Sun, L., Corvera, J., Gallick, G. E. and Kuang, J. (2006) Involvement of the adaptor protein Alix in actin cytoskeleton assembly. J. Biol. Chem. 285, 34640-34650
34. 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
35. Ono, A. and Freed, E. O. (1999) Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus. J. Virol. 73, 4136-4144
36. Spearman, P., Horton, R., Ratner, L. and Kuli-Zade, I. (1997) Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. J. Virol. 71, 6582-6592
37. Lee, Y. C., Block, G., Chen, H., Folch-Puy, E., Foronjy, R., Jalili, R., Jendresen, C. B., Kimura, M., Kraft, E., Lindemose, S. et al. (2008) One-step isolation of plasma membrane proteins using magnetic beads with immobilized concanavalin A. Protein Expression Purif. 62, 223-229
38. Pan, S., Wang, R., Zhou, X., Kloc, M., Corvera, J., Koomen, J., Kobayashi, R., Sifers, R., Gallick, G. E., Lin, S.-H. and Kuang, J. (2008) Extracellular Alix regulates integrin-mediated cell adhesions and extracellular matrix assembly. EMBO J. 27, 2077-2090
39. Rosenberg, I. M. (2004) Protein Analysis and Purification: Benchtop Techniques, Springer, New York
40. Newman, P. J., Kahn, R. A. and Hines, A. (1981) Detection and characterization of monoclonal antibodies to platelet membrane proteins. J. Cell Biol. 90, 249-253
41. Luhtala, N. and Odorizzi, G. (2004) Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes. J. Cell Biol. 166, 717-729
42. Mitin, N., Betts, L., Yohe, M. E., Der, C. J., Sondek, J. and Rossman, K. L. (2007) Release of autoinhibition of ASEF by APC leads to CDC42 activation and tumor suppression. Nat. Struct. Mol. Biol. 14, 814-823
43. Long, J. F., Feng, W., Wang, R., Chan, L. N., Ip, F. C., Xia, J., Ip, N. Y. and Zhang, M. (2005) Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat. Struct. Mol. Biol. 12, 722-728