Purification and architecture of the ubiquitous Wave complex

Alexis Gautreau; Hsin Yi H. Ho; Jiaxu Li; Hanno Steen; Steven P. Gygi; Marc W. Kirschner

doi:10.1073/pnas.0400628101

Purification and architecture of the ubiquitous Wave complex

Alexis Gautreau
, Hsin Yi H. Ho
, Jiaxu Li
, Hanno Steen
, Steven P. Gygi
, Marc W. Kirschner

Research output: Contribution to journal › Article › peer-review

Abstract

The Wave proteins are major activators of the Arp2/3 complex. The ubiquitous Wave-2 is required for actin polymerization at the leading edge of migrating cells. Here we purify Wave-2 from HeLa cells. Five proteins, Sra, Nap, Wave-2, Abi, and Hspc, are copurified, indicating that they form a tight complex. These proteins are only present in the complexed form, with the exception of Hspc, which displays a free pool. We reconstitute the Wave-2 complex by cotranslating in vitro the five subunits and use this system together with specific immunoprecipitations to study the molecular architecture of the complex. The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.

Original language	English
Pages (from-to)	4379-4383
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	101
Issue number	13
DOIs	https://doi.org/10.1073/pnas.0400628101
Publication status	Published - 30 Mar 2004
Externally published	Yes

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title = "Purification and architecture of the ubiquitous Wave complex",

abstract = "The Wave proteins are major activators of the Arp2/3 complex. The ubiquitous Wave-2 is required for actin polymerization at the leading edge of migrating cells. Here we purify Wave-2 from HeLa cells. Five proteins, Sra, Nap, Wave-2, Abi, and Hspc, are copurified, indicating that they form a tight complex. These proteins are only present in the complexed form, with the exception of Hspc, which displays a free pool. We reconstitute the Wave-2 complex by cotranslating in vitro the five subunits and use this system together with specific immunoprecipitations to study the molecular architecture of the complex. The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.",

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doi = "10.1073/pnas.0400628101",

language = "English",

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T1 - Purification and architecture of the ubiquitous Wave complex

AU - Gautreau, Alexis

AU - Ho, Hsin Yi H.

AU - Li, Jiaxu

AU - Steen, Hanno

AU - Gygi, Steven P.

AU - Kirschner, Marc W.

PY - 2004/3/30

Y1 - 2004/3/30

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AB - The Wave proteins are major activators of the Arp2/3 complex. The ubiquitous Wave-2 is required for actin polymerization at the leading edge of migrating cells. Here we purify Wave-2 from HeLa cells. Five proteins, Sra, Nap, Wave-2, Abi, and Hspc, are copurified, indicating that they form a tight complex. These proteins are only present in the complexed form, with the exception of Hspc, which displays a free pool. We reconstitute the Wave-2 complex by cotranslating in vitro the five subunits and use this system together with specific immunoprecipitations to study the molecular architecture of the complex. The complex is organized around a core of Nap and Abi. Sra is a peripheral subunit recruited on the Nap side, whereas the Wave and Hspc subunits are recruited on the Abi side of the core.

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DO - 10.1073/pnas.0400628101

M3 - Article

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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ER -

Purification and architecture of the ubiquitous Wave complex

Abstract

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