A role for p130Cas in mechanotransduction

Article Abstract:

Studies related to the sensitivity of focal adhesions to mechanical stimulation that is mediated by stretching of the adaptor protein p130Cas which enhances its phosphorylation by Src family kinases is reported. The findings implicate the adaptor protein p130Cas in adhesion-dependent mechanotransduction and also propose a compelling and comprehensive mechanism for force-driven signaling, whereby p130Cas, bound to the protein scaffold at local adhesions is subjected to stretching.

Phosphorylation, Cell adhesion

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Force sensing by mechanical extension of the Src family kinase substrate p130Cas

Article Abstract:

A remarkable enhancement of phosphorylation by Src family kinases with no apparent change in kinase activity was observed by mechanically extending bacterially expressed tyrosine phosphorylation of p130Cas (Cas). It is proposed based on the findings that Cas acts as a primary force sensor, transducing force into mechanical extension and thereby priming phosphorylation and activation of downstream signaling.

Tyrosine, Structure, Chemical properties, Guanosine triphosphatase, GTPases

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Periodic lamellipodial contractions correlate with rearward actin waves

Article Abstract:

Cellular lamellipodia bind to the matrix and probe its rigidity through forces generated by rearward F-actin transport. The conclusion indicates that an actin bound, contraction-activated signaling complex is transported locally from the tip to the base of the lamellipodium, activating the next contraction/extension cycle.

Actin

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