論文

査読有り
2016年3月

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

JOURNAL OF BIOLOGICAL CHEMISTRY
  • Kazumi Nomura
  • ,
  • Kimihide Hayakawa
  • ,
  • Hitoshi Tatsumi
  • ,
  • Shoichiro Ono

291
10
開始ページ
5146
終了ページ
5156
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M115.713495
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Actin-interacting protein 1 (AIP1) is a conserved WD repeat protein that promotes disassembly of actin filaments when actin-depolymerizing factor (ADF)/cofilin is present. Although AIP1 is known to be essential for a number of cellular events involving dynamic rearrangement of the actin cytoskeleton, the regulatory mechanism of the function of AIP1 is unknown. In this study, we report that two AIP1 isoforms from the nematode Caenorhabditis elegans, known as UNC-78 and AIPL-1, are pH-sensitive in enhancement of actin filament disassembly. Both AIP1 isoforms only weakly enhance disassembly of ADF/cofilin-bound actin filaments at an acidic pH but show stronger disassembly activity at neutral and basic pH values. However, a severing-defective mutant of UNC-78 shows pH-insensitive binding to ADF/cofilin-decorated actin filaments, suggesting that the process of filament severing or disassembly, but not filament binding, is pH-dependent. His-60 of AIP1 is located near the predicted binding surface for the ADF/cofilin-actin complex, and an H60K mutation of AIP1 partially impairs its pH sensitivity, suggesting that His-60 is involved in the pH sensor for AIP1. These biochemical results suggest that pH-dependent changes in AIP1 activity might be a novel regulatory mechanism of actin filament dynamics.

リンク情報
DOI
https://doi.org/10.1074/jbc.M115.713495
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000371640600027&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M115.713495
  • ISSN : 0021-9258
  • eISSN : 1083-351X
  • Web of Science ID : WOS:000371640600027

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