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Figure 5 | Cell Communication and Signaling

Figure 5

From: Distinct phosphorylation requirements regulate cortactin activation by TirEPEC and its binding to N-WASP

Figure 5

Model of cortactin action on EPEC pedestals. (A) Model of coordinated action by cortactin and N-WASP on EPEC pedestals. In theory, cortactin may bind Tir and N-WASP simultaneously, via its N-terminal and SH3 domain interaction respectively. EPEC-induced tyrosine phosphorylation of cortactin would terminate cortactin interaction with N-WASP but not with Tir. This could constitute a cyclical regulatory mechanism of actin polymerization on EPEC pedestals. Phosphotyrosine-cortactin might as well compete for the SH2 domain of Nck, thus uncoupling Tir from the Nck/N-WASP complex. (B) In the absence of N-WASP protein, cortactin would only interact with Tir, which would not be sufficient for pedestal formation.

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