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A single PXXP motif in the C-terminal region of srGAP3 mediates binding to multiple SH3 domains.

FEBS Lett.. 2015-04;  589(10):1156-63
Wuertenberger S, Groemping Y. Max Planck Institute for Developmental Biology, Department of Protein Evolution, Spemannstr. 35, D-72076 Tübingen, Germany
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摘要

The Slit-Robo GTPase-activating protein 3 (srGAP3) has been implicated in different critical aspects of neuronal development. These findings have mainly been based on the characterisation of the three conserved globular N-terminal domains, while the function of the C-terminal region (CTR) is still unknown. We show that this predicted unstructured region acts as an adaptor by binding to the endocytic proteins Amphiphysin, Endophilin-A2, Endophilin-A1, as well as the Ras signalling protein Grb2. All these interactions depend on a single proline-rich motif in the CTR and the Src-homology 3 domains of the binding partners. Via these interactions srGAP3 could link receptor signalling events to the endocytic machiner... More

关键词

Isothermal titration calorimetry; Mental disorder GAP; Protein-protein interaction; SH3 domain (adaptor); WAVE-associated RacGAP protein
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