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Zhang, Y. et al.

Assembly of the PINCH- ILK- CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites.

PINCH, integrin-linked kinase ( ILK) and calponin homology-containing ILK- binding protein ( CH-ILKBP) form a ternary complex that plays crucial roles at cell-extracellular matrix adhesion sites. To understand the mechanism underlying the complex formation and recruitment to cell-adhesion sites we have undertaken a combined structural, mutational and cell biological analysis. Three-dimensional structure-based point mutations identified specific PINCH and ILK sites that mediate the complex formation. Analyses of the binding defective point mutants revealed that the assembly of the PINCH- ILK- CH-ILKBP complex is essential for their localization to cell-extracellular matrix adhesion sites. The formation of the PINCH- ILK- CH-ILKBP complex precedes integrin-mediated cell adhesion and spreading. Furthermore, inhibition of protein kinase C, but not that of actin polymerization, inhibited the PINCH- ILK- CH-ILKBP complex formation, suggesting that the PINCH- ILK- CH-ILKBP complex likely serves as a downstream effector of protein kinase C in the cellular control of focal adhesion assembly. Finally, we provide evidence that the formation of the PINCH- ILK- CH-ILKBP complex, while necessary, is not sufficient for ILK localization to cell-extracellular matrix adhesion sites. These results provide new insights into the molecular mechanism underlying the assembly and regulation of cell-matrix adhesion structures.[1]

References

Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. Zhang, Y., Chen, K., Tu, Y., Velyvis, A., Yang, Y., Qin, J., Wu, C. J. Cell. Sci. (2002) [Pubmed]

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