Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages.
Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrin-vimentin complexes in macrophages.
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DOI：
10.1083/jcb.146.4.831
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发表时间：
1999-08-23
期刊：
影响因子：
--
通讯作者：
Matsudaira P
中科院分区：
文献类型：
--
作者：
Correia I;Chu D;Chou YH;Goldman RD;Matsudaira P
细胞通过与肌动蛋白细胞骨架相连的特殊结构附着在基质上。最近的研究报道，粘附也涉及到中间丝（IF）和微管细胞骨架，尽管它们的相互作用机制尚不清楚。在这里，我们报告了肌动蛋白和IF细胞骨架组分之间新的粘附依赖相互作用的证据。在生化分离实验中，使用特定于纤溶蛋白或纤溶蛋白的抗血清，从巨噬细胞的清洁剂提取物中共沉淀纤溶蛋白和纤溶蛋白。荧光显微镜证实了这种生化关联。在细胞粘附和扩散的早期阶段，这两种蛋白都与足小体共定位。丝状伪足和回缩纤维中也有这种复合物。洗涤剂提取后，足小体、丝状足和回缩纤维的纤蛋白和维蛋白染色消失，证实复合物定位于这些结构。纤维蛋白与血凝蛋白结合的1:4化学计量和低百分比（1%）的提取血凝蛋白表明，纤维蛋白与血凝蛋白亚基相互作用。在纤蛋白的nh2末端区域鉴定了一个纤蛋白结合位点，在纤蛋白CH1区域的143-188位残基上鉴定了纤蛋白结合位点。基于这些观察结果，我们提出纤蛋白-血凝蛋白复合物可能参与指导血凝蛋白细胞骨架在细胞粘附位点的组装。
Cells adhere to the substratum through specialized structures that are linked to the actin cytoskeleton. Recent studies report that adhesion also involves the intermediate filament (IF) and microtubule cytoskeletons, although their mechanisms of interaction are unknown. Here we report evidence for a novel adhesion-dependent interaction between components of the actin and IF cytoskeletons. In biochemical fractionation experiments, fimbrin and vimentin coprecipitate from detergent extracts of macrophages using vimentin- or fimbrin-specific antisera. Fluorescence microscopy confirms the biochemical association. Both proteins colocalized to podosomes in the earliest stages of cell adhesion and spreading. The complex is also found in filopodia and retraction fibers. After detergent extraction, fimbrin and vimentin staining of podosomes, filopodia, and retraction fibers are lost, confirming that the complex is localized to these structures. A 1:4 stoichiometry of fimbrin binding to vimentin and a low percentage (1%) of the extracted vimentin suggest that fimbrin interacts with a vimentin subunit. A fimbrin-binding site was identified in the NH2-terminal domain of vimentin and the vimentin binding site at residues 143–188 in the CH1 domain of fimbrin. Based on these observations, we propose that a fimbrin–vimentin complex may be involved in directing the assembly of the vimentin cytoskeleton at cell adhesion sites.
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影响因子：
4.8
作者：
Mabuchi, K;Li, B;Tao, T
通讯作者：
Tao, T
影响因子：
3.7
作者：
MARCHISIO, PC;CIRILLO, D;TARONE, G
通讯作者：
TARONE, G
影响因子：
2.5
作者：
CHAFEL, MM;SHEN, WY;MATSUDAIRA, P
通讯作者：
MATSUDAIRA, P
影响因子：
7.8
作者：
DePasquale, J A;Izzard, C S
通讯作者：
Izzard, C S
DOI：
10.1083/jcb.86.1.335
发表时间：
1980-07
期刊：
The Journal of cell biology
影响因子：
--
作者：
Bretscher A;Weber K
通讯作者：
Weber K