Open AccessTropomyosin Tm5NM1 Spatially Restricts Src Kinase Activity through Perturbation of Rab11 Vesicle Trafficking
Author(s) -
Cuc T. Bach,
Rachael Z. Murray,
Dylan M. Owen,
Katharina Gaus,
Geraldine M. O’Neill
Publication year - 2014
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.00796-14
Subject(s) - focal adhesion , fluorescence recovery after photobleaching , microbiology and biotechnology , biology , tropomyosin , actin , proto oncogene tyrosine protein kinase src , actin cytoskeleton , ptk2 , cytoskeleton , endosome , phosphorylation , protein kinase a , biochemistry , cell , mitogen activated protein kinase kinase , membrane , intracellular
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.
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