2. Academic Validation
  3. AIP1/WDR1 supports mitotic cell rounding

AIP1/WDR1 supports mitotic cell rounding

  • Biochem Biophys Res Commun. 2005 Feb 4;327(1):268-75. doi: 10.1016/j.bbrc.2004.11.156.
Taketsugu Fujibuchi 1,  Yasuhito Abe,  Takashi Takeuchi,  Yoshinori Imai,  Yoshiaki Kamei,  Ryuichi Murase,  Norifumi Ueda,  Kazuhiro Shigemoto,  Haruyasu Yamamoto,  Katsumi Kito
Affiliations

Affiliation

  • 1 Division of Molecular Pathology, Department of Pathology, National University Corporation, Ehime University School of Medicine, Toh-on, Ehime 791-0295, Japan.
PMID: 15629458 DOI: 10.1016/j.bbrc.2004.11.156
Abstract

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.

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