Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.
Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.
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DOI：
10.1242/jcs.189878
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发表时间：
2016-12-01
影响因子：
4
通讯作者：
Brown NH
中科院分区：
文献类型：
--
作者：
Maartens AP;Wellmann J;Wictome E;Klapholz B;Green H;Brown NH
Vinculin is a highly conserved protein involved in cell adhesion and mechanotransduction, and both gain and loss of its activity causes defective cell behaviour. Here, we examine how altering vinculin activity perturbs integrin function within the context of Drosophila development. Whereas loss of vinculin produced relatively minor phenotypes, gain of vinculin activity, through a loss of head–tail autoinhibition, caused lethality. The minimal domain capable of inducing lethality is the talin-binding D1 domain, and this appears to require talin-binding activity, as lethality was suppressed by competition with single vinculin-binding sites from talin. Activated Drosophila vinculin triggered the formation of cytoplasmic adhesion complexes through the rod of talin, but independently of integrin. These complexes contain a subset of adhesion proteins but no longer link the membrane to actin. The negative effects of hyperactive vinculin were segregated into morphogenetic defects caused by its whole head domain and lethality caused by its D1 domain. These findings demonstrate the crucial importance of the tight control of the activity of vinculin. Summary: Development is more sensitive to gain of vinculin activity than its loss, and vinculin can promote cytoplasmic adhesion complexes independently of the usual integrin cue.
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影响因子：
64.5
作者：
BOGAERT, T;BROWN, N;WILCOX, M
通讯作者：
WILCOX, M
影响因子：
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WATERSTON, RH
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4.8
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通讯作者：
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