Abstract

Cortactin, a substrate of sarcoma (Src) kinases, is an actin-binding protein that is involved in cytoskeletal regulation, and is frequently overexpressed in cancer cells. Binding to the actin related protein 2/3 (Arp2/3) complex stimulates cortactin activity, which promotes F-actin nucleation and assembly. Cortactin promotes cancer cell migration and invasion, and plays a pivotal role in invadopodia formation and extra cellular matrix degradation. Overexpression of cortactin, by amplification of the chromosomal band 11q13, increases tumor aggressiveness. In this review, we report on the current knowledge and potential mechanisms of action of cortactin as a critical mediator of cancer cell migration and invasion.

Highlights

  • Cortactin, a prominent actin-binding protein, was initially character as a component of the Src non-receptor tyrosine kinase pp60src

  • We report on the current knowledge and potential mechanisms of action of cortactin as a critical mediator of cancer cell migration and invasion

  • Cortactin is critical for membrane trafficking and promotes the secretion of extracellular matrix (ECM)-degrading proteinases, which are crucial for the invadopodia formation and its function in tumor cell metastasis

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Summary

Introduction

A prominent actin-binding protein, was initially character as a component of the Src non-receptor tyrosine kinase pp60src. A substrate of sarcoma (Src) kinases, is an actin-binding protein that is involved in cytoskeletal regulation, and is frequently overexpressed in cancer cells.

Results
Conclusion
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