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.
This research was originally published in the Journal of Biological Chemistry 281, no. 28 (2006): 19196-19203. © the American Society for Biochemistry and Molecular Biology
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