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Abstract
In order for cells to stop moving, they must synchronously stabilize actin filaments and their associated focal adhesions. How these two structures are coordinated in time and space is not known. We show here that the actin association protein Tm5NM1, which induces stable actin filaments, concurrently suppresses the trafficking of focal-adhesion-regulatory molecules. Using combinations of fluorescent biosensors and fluorescence recovery after photobleaching (FRAP), we demonstrate that Tm5NM1 reduces the level of delivery of Src kinase to focal adhesions, resulting in reduced phosphorylation of adhesion-resident Src substrates. Live imaging of Rab11-positive recycling endosomes that carry Src to focal adhesions reveals disruption of this pathway. We propose that tropomyosin synchronizes adhesion dynamics with the cytoskeleton by regulating actin-dependent trafficking of essential focal-adhesion molecules.
SUPPLEMENTAL MATERIAL
Supplemental material for this article may be found at http://dx.doi.org/10.1128/MCB.00796-14.
ACKNOWLEDGMENTS
We acknowledge Jessie Zhong for assistance with immunofluorescence staining.
This work was supported by National Health and Medical Research Council grant 512251 (to G.M.O.) and by Australian Research Council Discovery Projects DP130100269 (to K.G. and G.M.O.) and DP1095468 (to K.G. and D.O.). C.T.B. was supported by a C4-Fellowship from The Kids Cancer Project.