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肌动蛋白相互作用蛋白1积极拆解肌动蛋白解聚因子/丝切蛋白结合的肌动蛋白丝的微观证据。

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

作者信息

Ono Shoichiro, Mohri Kurato, Ono Kanako

机构信息

Department of Pathology, Emory University, Atlanta, Georgia 30322, USA.

出版信息

J Biol Chem. 2004 Apr 2;279(14):14207-12. doi: 10.1074/jbc.M313418200. Epub 2004 Jan 23.

DOI:10.1074/jbc.M313418200
PMID:14742433
Abstract

Actin-depolymerizing factor (ADF)/cofilin and gelsolin are the two major factors to enhance actin filament disassembly. Actin-interacting protein 1 (AIP1) enhances fragmentation of ADF/cofilin-bound filaments and caps the barbed ends. However, the mechanism by which AIP1 disassembles ADF/cofilin-bound filaments is not clearly understood. Here, we directly observed the effects of these proteins on filamentous actin by fluorescence microscopy and gained novel insight into the function of ADF/cofilin and AIP1. ADF/cofilin severed filaments and AIP1 strongly enhanced disassembly at nanomolar concentrations. However, gelsolin, gelsolin-actin complex, or cytochalasin D did not enhance disassembly by ADF/cofilin, suggesting that the strong activity of AIP1 cannot be explained by simple barbed end capping. Barbed end capping by ADF/cofilin and AIP1 was weak and allowed filament elongation, whereas gelsolin or gelsolin-actin complex strongly capped and inhibited elongation. These results suggest that AIP has an active role in filament severing or depolymerization and that ADF/cofilin and AIP1 are distinct from gelsolin in modulating filament elongation.

摘要

肌动蛋白解聚因子（ADF）/丝切蛋白和凝溶胶蛋白是增强肌动蛋白丝解聚的两个主要因素。肌动蛋白相互作用蛋白1（AIP1）可增强与ADF/丝切蛋白结合的肌动蛋白丝的片段化，并封闭肌动蛋白丝的尖端。然而，AIP1拆解与ADF/丝切蛋白结合的肌动蛋白丝的机制尚不清楚。在这里，我们通过荧光显微镜直接观察了这些蛋白质对丝状肌动蛋白的影响，并对ADF/丝切蛋白和AIP1的功能有了新的认识。ADF/丝切蛋白切断肌动蛋白丝，AIP1在纳摩尔浓度下能强烈增强解聚。然而，凝溶胶蛋白、凝溶胶蛋白-肌动蛋白复合物或细胞松弛素D并不能增强ADF/丝切蛋白介导的解聚，这表明AIP1的强大活性不能简单地用封闭肌动蛋白丝尖端来解释。ADF/丝切蛋白和AIP1对肌动蛋白丝尖端的封闭作用较弱，能使肌动蛋白丝延长，而凝溶胶蛋白或凝溶胶蛋白-肌动蛋白复合物则能强烈封闭并抑制其延长。这些结果表明，AIP在肌动蛋白丝切断或解聚过程中发挥着积极作用，并且ADF/丝切蛋白和AIP1在调节肌动蛋白丝延长方面与凝溶胶蛋白不同。

相似文献

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

J Biol Chem. 2004-4-2

[2]
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

[3]
Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle.

Mol Biol Cell. 2006-5

[4]
Actin-interacting Protein 1 Promotes Disassembly of Actin-depolymerizing Factor/Cofilin-bound Actin Filaments in a pH-dependent Manner.

J Biol Chem. 2016-3-4

[5]
ADF/Cofilin Accelerates Actin Dynamics by Severing Filaments and Promoting Their Depolymerization at Both Ends.

Curr Biol. 2017-6-15

[6]
Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.

Biochemistry. 2003-11-25

[7]
Architecture dependence of actin filament network disassembly.

Curr Biol. 2015-6-1

[8]
Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform.

J Cell Sci. 2003-10-15

[9]
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

[10]
The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization.

Biochemistry. 2005-11-1

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[2]
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[3]
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[4]
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[5]
Real-Time Single-Molecule Kinetic Analyses of AIP1-Enhanced Actin Filament Severing in the Presence of Cofilin.

J Mol Biol. 2018-11-12

[6]
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[7]
Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.

Mol Biol Cell. 2018-3-30

[8]
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

[9]
Peptide regulation of cofilin activity in the CNS: A novel therapeutic approach for treatment of multiple neurological disorders.

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[10]
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