Adhesion signaling by a novel mitotic substrate of src kinases.

Article Details

Citation

Bhatt AS, Erdjument-Bromage H, Tempst P, Craik CS, Moasser MM

Adhesion signaling by a novel mitotic substrate of src kinases.

Oncogene. 2005 Aug 11;24(34):5333-43.

PubMed ID
16007225 [ View in PubMed
]
Abstract

Src kinases are activated and relocalize to the cytoplasm during mitosis, but their mitotic function has remained elusive. We describe here a novel mitotic substrate of src kinases. Trask (transmembrane and associated with src kinases) is a 140 kDa type I transmembrane glycoprotein unrelated to currently known protein families. Src kinases phosphorylate Trask in vitro and mediate its mitotic hyperphosphorylation in vivo. Trask associates with both yes and src, is localized to the cell membrane during interphase, and undergoes cytoplasmic relocalization during mitosis. Overexpression of Trask leads to cell rounding and a loss of adhesion phenotype. Consistent with a function in cell adhesion, Trask interacts with a number of adhesion and matrix proteins including cadherins, syndecans, and the membrane-type serine protease 1 (MT-SP1), and is proteolytically cleaved by MT-SP1. Trask is unique among cell adhesion molecules in that it is under cell cycle regulation and thus links src kinases with the mitotic regulation of cell adhesion. This suggests a potential pathway by which hyperactive src kinases in tumors can deregulate adhesion signaling and mediate the metastatic phenotype.

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Polypeptides
NameUniProt ID
Suppressor of tumorigenicity 14 proteinQ9Y5Y6Details