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生化和遗传分析有助于深入了解酿酒酵母中Aip1p-丝切蛋白复合物对肌动蛋白丝拆卸的结构和机制特性。

Biochemical and genetic analyses provide insight into the structural and mechanistic properties of actin filament disassembly by the Aip1p cofilin complex in Saccharomyces cerevisiae.

作者信息

Clark Michael G, Amberg David C

机构信息

Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, New York 13210, USA.

出版信息

Genetics. 2007 Jul;176(3):1527-39. doi: 10.1534/genetics.107.072066. Epub 2007 May 4.

DOI:10.1534/genetics.107.072066
PMID:17483419
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1931519/
Abstract

Explication of the Aip1p/cofilin/actin filament complex may lead to a more detailed understanding of the mechanisms by which Aip1p and cofilin collaborate to rapidly disassemble filaments. We further characterized the actin-Aip1p interface through a random mutagenic screen of ACT1, identifying a novel Aip1p interaction site on actin. This finding is consistent with our current ternary complex model and offers insights into how Aip1p may disturb intersubunit contacts within an actin filament. In addition, site-directed mutagenesis aimed at interfering with salt bridge interactions at the predicted Aip1p-cofilin interface revealed hyperactive alleles of cof1 and aip1 that support the ternary complex model and suggest that conformational changes in cofilin structure may be transmitted to actin filaments, causing increased destabilization. Furthermore, these data support an active role for Aip1p in promoting actin filament turnover.

摘要

对Aip1p/丝切蛋白/肌动蛋白丝复合物的阐释可能会使我们更详细地了解Aip1p和丝切蛋白协同作用以快速拆解肌动蛋白丝的机制。我们通过对ACT1进行随机诱变筛选，进一步表征了肌动蛋白与Aip1p的界面，确定了肌动蛋白上一个新的Aip1p相互作用位点。这一发现与我们当前的三元复合物模型一致，并为Aip1p如何干扰肌动蛋白丝内的亚基间接触提供了见解。此外，旨在干扰预测的Aip1p-丝切蛋白界面处盐桥相互作用的定点诱变揭示了cof1和aip1的高活性等位基因，这些等位基因支持三元复合物模型，并表明丝切蛋白结构的构象变化可能传递至肌动蛋白丝，导致稳定性增加。此外，这些数据支持Aip1p在促进肌动蛋白丝周转中发挥积极作用。

相似文献

[1]
Biochemical and genetic analyses provide insight into the structural and mechanistic properties of actin filament disassembly by the Aip1p cofilin complex in Saccharomyces cerevisiae.

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[2]
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引用本文的文献

[1]
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J Biol Chem. 2020-9-18

[2]
Functions of actin-interacting protein 1 (AIP1)/WD repeat protein 1 (WDR1) in actin filament dynamics and cytoskeletal regulation.

Biochem Biophys Res Commun. 2017-10-19

[3]
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Cell Death Dis. 2015-7-16

[4]
Aip1 destabilizes cofilin-saturated actin filaments by severing and accelerating monomer dissociation from ends.

Curr Biol. 2014-12-1

[5]
Coordination of the filament stabilizing versus destabilizing activities of cofilin through its secondary binding site on actin.

Cytoskeleton (Hoboken). 2014-6

[6]
Linking genetics to structural biology: complex heterozygosity screening with actin alanine scan alleles identifies functionally related surfaces on yeast actin.

G3 (Bethesda). 2014-6-17

[7]
Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p.

J Biol Chem. 2013-5-7

[8]
Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.

Mol Biol Cell. 2012-5-2

[9]
Novel interactions between actin and the proteasome revealed by complex haploinsufficiency.

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[10]
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本文引用的文献

[1]
Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1.

J Cell Biol. 2006-10-23

[2]
Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin.

Mol Cell. 2006-10-6

[3]
Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments.

Mol Biol Cell. 2006-7

[4]
A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities.

Mol Biol Cell. 2006-4

[5]
Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.

J Biol Chem. 2004-7-23

[6]
Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin filaments.

J Biol Chem. 2004-4-2

[7]
The actin-interacting protein AIP1 is essential for actin organization and plant development.

Curr Biol. 2004-1-20

[8]
Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1.

Curr Biol. 2003-12-16

[9]
ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments.

J Cell Biol. 2003-12-8

[10]
Actin-binding proteins required for reliable chromosome segregation in mitosis.

Cell Motil Cytoskeleton. 2004-1

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