The Yeast AAA+ Chaperone Hsp104 Is Part of a Network That Links the Actin Cytoskeleton with the Inheritance of Damaged Proteins

被引：63

作者：

Tessarz, Peter ^{[1
]}

Schwarz, Michael ^{[2
]}

Mogk, Axel ^{[1
]}

Bukau, Bernd ^{[1
]}

机构：

[1] Univ Heidelberg, Zentrum Mol Biol Heidelberg, DKFZ ZMBH Alliance, D-69120 Heidelberg, Germany

[2] Max Planck Inst Biochem, Dept Mol Cell Biol, D-82152 Martinsried, Germany

来源：

MOLECULAR AND CELLULAR BIOLOGY | 2009年 / 29卷 / 13期

关键词：

SACCHAROMYCES-CEREVISIAE; CELL POLARITY; SHUTTLE VECTORS; CENTRAL PORE; SYSTEM; GENES; CYTOKINESIS; EXPRESSION; MECHANISM; CLPB;

D O I：

10.1128/MCB.00201-09

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions. Recently, Hsp104, together with the actin cytoskeleton, has been implicated in the asymmetric distribution of carbonylated proteins. Here, we investigated the interplay between Hsp104 and actin by using a dominant-negative variant of Hsp104 (HAP/ClpP) that degrades substrate proteins instead of remodeling them. Coexpression of HAP/ClpP causes defects in morphology and the actin cytoskeleton. Taking a candidate approach, we identified Spa2, a member of the polarisome complex, as an Hsp104 substrate. Furthermore, we provided genetic evidence that links Spa2 and Hsp104 to Hof1, a member of the cytokinesis machinery. Spa2 and Hof1 knockout cells are affected in the asymmetric distribution of damaged proteins, suggesting that Hsp104, Spa2, and Hof1 are members of a network controlling the inheritance of carbonylated proteins.

引用

页码：3738 / 3745

页数：8

共 41 条

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