2009年7月
Regulation of Cellular Contractile Force in Response to Mechanical Stretch by Diphosphorylation of Myosin Regulatory Light Chain via RhoA Signaling Cascade
CELL MOTILITY AND THE CYTOSKELETON
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- 巻
- 66
- 号
- 7
- 開始ページ
- 389
- 終了ページ
- 397
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/cm.20378
- 出版者・発行元
- WILEY-LISS
Fibroblasts regulate their contractile force in response to external stretch; however, the detailed mechanism by which the force is regulated is unclear. Here, we show that diphosphorylation and dephosphorylation of myosin regulatory light chain (MRLC) are involved in the stretch-induced force response. Cellular stiffness, which reflects the cellular contractile force, under external stretch was measured by mechanical-scanning probe microscopy. Fibroblasts (NIH-3T3) expressing green fluorescent protein (GFP)-tagged mutant-type MRLC (MRLC(T18A)-GFP), which cannot be diphosphorylated, did not show any stretch-induced stiffness response, whereas the stiffness in cells expressing GFP-tagged wild-type MRLC(MRLC(WT)-GFP) increased immediately after the stretch and subsequently decreased after 1-2 h. Urea-PAGE western blot analysis showed that the proportion of diphosphorylated MRLC (PP-MRLC) transiently increased after the stretch and decreased after 1-2 h. Dominant-negative RhoA (RhoA(N19))-expressing cells did not show the stiffness response to the stretch, whereas wild-type RhoA-expressing cells did. It was concluded that file Cellular force response originates in the stretch-induced diphosphorylation and dephosphorylation of MRLC and is regulated via the RhoA signaling cascade Cell Motil. Cytoskeleton 66: 389-397,2009. (C) 2009 Wiley-Liss, Inc.
- リンク情報
- ID情報
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- DOI : 10.1002/cm.20378
- ISSN : 0886-1544
- Web of Science ID : WOS:000267583400004