Syndapins integrate N-WASP in receptor-mediated endocytosis.
Syndapins are potential links between the cortical actin cytoskeleton and endocytosis because this family of dynamin- associated proteins can also interact with the Arp2/3 complex activator N-WASP. Here we provide evidence for involvement of N-WASP interactions in receptor-mediated endocytosis. We reveal that the observed dominant-negative effects of N-WASP are dependent exclusively on the proline-rich domain, the binding interface of syndapins. Our results therefore suggest that syndapins integrate N-WASP functions in endocytosis. Both proteins co-localize in neuronal cells. Consistent with a crucial role for syndapins in endocytic uptake, co-overexpression of syndapins rescued the endocytosis block caused by N-WASP. An in vivo reconstitution of the syndapin- N-WASP interaction at cellular membranes triggered local actin polymerization. Depletion of endogenous N-WASP by sequestering it to mitochondria or by introducing anti-N-WASP antibodies impaired endocytosis. Our data suggest that syndapins may act as important coordinators of N-WASP and dynamin functions during the different steps of receptor- mediated endocytosis and that local actin polymerization induced by syndapin- N-WASP interactions may be a mechanism supporting clathrin-coated vesicle detachment and movement away from the plasma membrane.[1]References
- Syndapins integrate N-WASP in receptor-mediated endocytosis. Kessels, M.M., Qualmann, B. EMBO J. (2002) [Pubmed]
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