Calcium/calmodulin-dependent protein kinase II controls integrin α5β1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1α
Calcium/calmodulin-dependent protein kinase II controls integrin α5β1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1α
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DOI：
10.1006/bbrc.1998.9592
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发表时间：
1998-11-09
影响因子：
3.1
通讯作者：
Block, MR
中科院分区：
文献类型：
--
作者：
Bouvard, D;Block, MR
本文提供的证据表明，钙/钙调素依赖性蛋白激酶II（CaMK II）的CHO细胞粘附在纤连蛋白的调节是通过最近描述的整合素胞质结构域相关蛋白-1 α（ICAP-1 α）介导的。位于ICAP-1 α的最佳CaMKII识别基序内的点突变T38 D导致细胞扩散的强烈缺陷，这不能通过抑制内源性CaMKII来克服。这一事实有力地表明，CaMK Ⅱ对Threatin 38的磷酸化调节α（5）β（1）整联蛋白的功能。相反，突变T38 A产生ICAP-1 α的类似物，其不能被磷酸化，并且当CaMKII被抑制时，其刺激细胞在纤连蛋白上扩散至类似程度，（C）1998 Academic Press。
This paper provided evidence that the regulation of CHO cell adhesion on fibronectin by calcium/calmodulin-dependent protein kinase II (CaMKII) is mediated through the recently described integrin cytoplasmic domain associated protein-1 alpha (ICAP-1 alpha). The point mutation T38D localized within the optimal CaMKII recognition motif of ICAP-1 alpha results in a strong defect in cell spreading which cannot be overcome by the inhibition of the endogenous CaMKII. This fact strongly suggests that the phosphorylation of Threonine 38 by CaMKII modulates the alpha(5)beta(1) integrin function. Conversely, the mutation T38A produces an analog of ICAP-1 alpha that cannot be phosphorylated and that stimulates cell spreading on fibronectin to a similar extent when CaMKII is inhibited, (C) 1998 Academic Press.