このエントリーをはてなブックマークに追加
ID 34807
本文ファイル
著者
Kondo, Tomo
Itakura, Shiho
Hosoya, Hiroshi
キーワード
Myosin II regulatory light chain
Actin
Contractile ring
Cytokinesis
Phosphorylation
NDC
生物科学・一般生物学
抄録(英)
During cytokinesis in eukaryotic cells, an actomyosin-based contractile ring (CR) is assembled along the equator of the cell. Myosin II ATPase activity is stimulated by the phosphorylation of the myosin II regulatory light chain (MRLC) in vitro, and phosphorylated MRLC localizes at the CR in various types of cells. Previous studies have determined that phosphorylated MRLC plays an important role in CR furrowing. However, the role of phosphorylated MRLC in CR assembly remains unknown. Here, we have used confocal microscopy to observe dividing HeLa cells expressing fluorescent protein-tagged MRLC mutants and actin during CR assembly near the cortex. Di-phosphomimic MRLC accumulated at the cell equator earlier than non-phosphorylatable MRLC and actin. Interestingly, perturbation of myosin II activity by non-phosphorylatable MRLC expression or treatment with blebbistatin, a myosin II inhibitor, did not alter the time of actin accumulation at the cell equator. Furthermore, inhibition of actin polymerization by treatment with latrunculin A had no effect on MRLC accumulation at the cell equator. Taken together, these data suggest that phosphorylated MRLC temporally controls its own accumulation, but not that of actin, in cultured mammalian cells.
掲載誌名
Experimental Cell Research
318巻
8号
開始ページ
915
終了ページ
924
出版年月日
2012
出版者
Elsevier Inc.
ISSN
0006-291X
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
(c) 2012 Elsevier Inc. All rights reserved.
関連情報URL
部局名
理学研究科