Structural basis of Vta1 function in the multivesicular body sorting pathway

被引：89

作者：

Xiao, Junyu ^{[1
,2
]}

Xia, Hengchuan ^{[1
,2
]}

Zhou, Jiahai ^{[1
,2
]}

Azmi, Ishara F. ^{[3
]}

Davies, Brian A. ^{[3
]}

Katzmann, David J. ^{[3
]}

Xu, Zhaohui ^{[1
,2
]}

机构：

[1] Univ Michigan, Sch Med, Inst Life Sci, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA

[3] Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

来源：

DEVELOPMENTAL CELL | 2008年 / 14卷 / 01期

关键词：

D O I：

10.1016/j.devcel.2007.10.013

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1 dimerization and both subunits are required for its function as a Vps4 regulator. Emerging from our analysis is a mechanism of regulation by Vta1 in which the C-terminal domain stabilizes the ATP-dependent double ring assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4 disassembly machinery and the accessory ESCRT-III proteins. This provides an additional level of regulation and coordination for ESCRT-III assembly and disassembly.

引用

页码：37 / 49

页数：13

共 34 条

[11] The Arabidopsis AAA ATPase SKD1 is involved in multivesicular endosome function and interacts with its positive regulator LYST-INTERACTING PROTEIN5 [J].

Haas, Thomas J. ;

Sliwinski, Marek K. ;

Martinez, Dana E. ;

Preuss, Mary ;

Ebine, Kazuo ;

Ueda, Takashi ;

Nielsen, Erik ;

Odorizzi, Greg ;

Otegui, Marisa S. .

PLANT CELL, 2007, 19 (04) :1295-1312

[12]

HUANG TG, 1994, J BIOL CHEM, V269, P16493

[13] The ESCRT complexes: Structure and mechanism of a membrane-trafficking network [J].

Hurley, James H. ;

Emr, Scott D. .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 2006, 35 :277-298

[14] IMPROVED METHODS FOR BUILDING PROTEIN MODELS IN ELECTRON-DENSITY MAPS AND THE LOCATION OF ERRORS IN THESE MODELS [J].

JONES, TA ;

ZOU, JY ;

COWAN, SW ;

KJELDGAARD, M .

ACTA CRYSTALLOGRAPHICA SECTION A, 1991, 47 :110-119

[15] Receptor downregulation and multivesicular-body sorting [J].

Katzmann, DJ ;

Odorizzi, G ;

Emr, SD .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2002, 3 (12) :893-905

[16] Vta1p and Vps46p regulate the membrane association and ATPase activity of Vps4p at the yeast multivesicular body [J].

Lottridge, JM ;

Flannery, AR ;

Vincelli, JL ;

Stevens, TH .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (16) :6202-6207

[17] Retrovirus budding [J].

Morita, E ;

Sundquist, WI .

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2004, 20 :395-425

[18] Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis [J].

Morita, Eiji ;

Sandrin, Virginie ;

Chung, Hyo-Young ;

Morham, Scott G. ;

Gygi, Steven P. ;

Rodesch, Christopher K. ;

Sundquist, Wesley I. .

EMBO JOURNAL, 2007, 26 (19) :4215-4227

[19] ARP/wARP and automatic interpretation of protein electron density maps [J].

Morris, RJ ;

Perrakis, A ;

Lamzin, VS .

MACROMOLECULAR CRYSTALLOGRAPHY, PT D, 2003, 374 :229-244

[20] Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4 [J].

Obita, Takayuki ;

Saksena, Suraj ;

Ghazi-Tabatabai, Sara ;

Gill, David J. ;

Perisic, Olga ;

Emr, Scott D. ;

Williams, Roger L. .

NATURE, 2007, 449 (7163) :735-U11

← 1 2 3 4 →