2005年2月
AIP1/WDR1 supports mitotic cell rounding
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 327
- 号
- 1
- 開始ページ
- 268
- 終了ページ
- 275
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1016/j.bbrc.2004.11.156
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
The actin cytoskeleton plays a fundamental role in configuring cell shapes and movements. Actin interacting protein 1 (AIP1)/ tryptophan-aspartate-repeat protein 1 (WDR1) induces actin severing and disassembly cooperating with ADF/cofilin. We found that mitotic cell flattening but not rounding was manifested by suppression of AIP1/WDR1 in cells. This mitotic cell flattening was not due to any changes in phosphorylation and distribution of cofilin in cells. We carried out a direct observation of actin filament severing/disassembly assay and found that phosphorylated cofilin still somewhat severs/disassembles actin filaments and that AIP1/WDR1 effaces this in vitro. We suggest that the phosphorylation of ADF/cofilin will be insufficient to completely inhibit actin turnover during mitosis, and that AIP1/WDR1 could abort the severing/disassembly activity somewhat still carried out due to phosphorylated ADF/cofilin. This mechanism could be required to induce cell morphologic changes, especially mitotic cell rounding. (C) 2004 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2004.11.156
- ISSN : 0006-291X
- PubMed ID : 15629458
- Web of Science ID : WOS:000226345400039