Involvement of Fyn tyrosine kinase in actin stress fiber formation in fibroblasts
Involvement of Fyn tyrosine kinase in actin stress fiber formation in fibroblasts
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DOI：
10.1016/j.febslet.2007.10.010
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发表时间：
2007-11-13
期刊：
影响因子：
3.5
通讯作者：
Kobayashi, Sei
中科院分区：
文献类型：
--
作者：
Xu, Dan;Kishi, Hiroko;Kobayashi, Sei
溶血磷脂酸（LPA）和鞘氨醇磷酸胆碱（SPC）激活Fyn酪氨酸激酶并诱导应激纤维形成，这可通过Fyn的药理学抑制、Fyn的基因沉默或显性阴性Fyn来阻断。过度表达的组成性活性Fyn定位在F-肌动蛋白束的两端，并触发应力纤维的形成，只有后者被废除的Rho激酶（ROCK）抑制。SPC，而不是LPA，诱导丝状伪足样突起的形成，这是不介导的Fyn和ROCK。因此，Fyn似乎作用于LPA和SPC的下游，以特异性地刺激成纤维细胞中由ROCK介导的应力纤维形成。(C)2007年由Elsevier B出版。V.代表欧洲生物化学学会联合会。
Lysophosphatidic acid (LPA) and sphingosylphosphorylcholine (SPC) activated Fyn tyrosine kinase and induced stress fiber formation, which was blocked by pharmacological inhibition of Fyn, gene silencing of Fyn, or dominant negative Fyn. Overexpressed constitutively active Fyn localized at both ends of F-actin bundles and triggered stress fiber formation, only the latter of which was abolished by Rho-kinase (ROCK) inhibition. SPC, but not LPA, induced filopodia-like protrusion formation, which was not mediated by Fyn and ROCK. Thus, Fyn appears to act downstream of LPA and SPC to specifically stimulate stress fiber formation mediated by ROCK in fibroblasts. (C) 2007 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.