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Fig. 9 | Cell Communication and Signaling

Fig. 9

From: The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function

Fig. 9

Model of Shp1-dependent regulation of invadopodia. Schematic representation of an A375MM melanoma cell with ventral invadopodia degrading the extracellular matrix (ECM). Cortactin phosphorylation on tyrosine 421 results in disruption of the inhibitory interaction between cortactin and cofilin with the recruitment and activation of multiple components of the actin regulatory machinery (N-WASP, Arp2/3, Nck1) to promote actin polymerization, matrix-metalloproteasis (MMP) recruitment and efficient invadopodial matrix degradation. The GroPIns (G) binds to Shp1 and induces its localization at invadopodia. This leads to cortactin dephosphorylation at tyrosine 421, with a consequent impairment of cortactin scaffolding-activity, invadopodia disassembly and reduced cancer cell invasion. See text for details

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