CD2-associated protein (CD2AP) is a scaffold molecule that plays a critical role in the maintenance of the kidney filtration barrier. Little, however, is understood about its mechanism of function. We used mass spectrometry to identify CD2AP-interacting proteins. Many of the proteins that we identified suggest a role for CD2AP in endocytosis and actin regulation. To address the role of CD2AP in regulation of the actin cytoskeleton, we focused on characterizing the interaction of CD2AP with actin-capping protein CP. We identified a novel binding motif LXHXTXXRPK(X)6P present in CD2AP that is also found in its homolog Cin85 and other capping protein-associated proteins such as CARMIL and CKIP-1. CD2AP inhibits the function of capping protein in vitro. Therefore, our results support a role of CD2AP in the regulation of the actin cytoskeleton.
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Bruck, Serawit, Tobias B. Huber, Robert J. Ingham, Kyoungtae Kim, Hanspeter Niederstrasser, Paul M. Allen, Tony Pawson, John A. Cooper, and Andrey S. Shaw. "Identification of a novel inhibitory actin-capping protein binding motif in CD2-associated protein." Journal of Biological Chemistry 281, no. 28 (2006): 19196-19203.
Journal of Biological Chemistry