Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength.
Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength.
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DOI:
10.1242/jcs.043042
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发表时间:
2009-05-01
影响因子:
4
通讯作者:
Jones JC
中科院分区:
文献类型:
--
作者:
Bhattacharya R;Gonzalez AM;Debiase PJ;Trejo HE;Goldman RD;Flitney FW;Jones JC
Much effort has been expended on analyzing how microfilament and microtubule cytoskeletons dictate the interaction of cells with matrix at adhesive sites called focal adhesions (FAs). However, vimentin intermediate filaments (IFs) also associate with the cell surface at FAs in endothelial cells. Here, we show that IF recruitment to FAs in endothelial cells requires β3 integrin, plectin and the microtubule cytoskeleton, and is dependent on microtubule motors. In CHO cells, which lack β3 integrin but contain vimentin, IFs appear to be collapsed around the nucleus, whereas in CHO cells expressing β3 integrin (CHOwtβ3), vimentin IFs extend to FAs at the cell periphery. This recruitment is regulated by tyrosine residues in the β3 integrin cytoplasmic tail. Moreover, CHOwtβ3 cells exhibit significantly greater adhesive strength than CHO or CHO cells expressing mutated β3 integrin proteins. These differences require an intact vimentin network. Therefore, vimentin IF recruitment to the cell surface is tightly regulated and modulates the strength of adhesion of cells to their substrate.
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