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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: Cell Signal. 2011 Jun 13;23(11):1691–1697. doi: 10.1016/j.cellsig.2011.06.004

Figure 1. Schematic representation of TRIP6.

Figure 1

The N-terminal half of TRIP6 contains a proline-rich region with multiple PXXP motifs, a Crm-1-dependent nuclear export signal, and a phosphotyrosine-55-directed pYXXP motif that serves as a docking site for Crk SH2 domain. The carboxyl-terminal half of TRIP6 contains three tandem LIM domains and a PDZ-binding motif. These multiple elements allow TRIP6 to serve as an adaptor for a wide variety of partners with diverse functional outcomes.