Key result
The actin association protein Tm5NM1 reduces the delivery of Src kinase to focal adhesions by disrupting Rab11 vesicle trafficking, leading to reduced phosphorylation of Src substrates.
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Does not yet guide clinical Src targeting; leaves open Tm5NM1 as a potential modulator of focal adhesion signaling.
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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Bach et al. (2014) studied this question. Tm5NM1 was evaluated on Src kinase delivery to focal adhesions and phosphorylation of Src substrates. The actin association protein Tm5NM1 reduces the delivery of Src kinase to focal adhesions by disrupting Rab11 vesicle trafficking, leading to reduced phosphorylation of Src substrates.
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