Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 281, Issue 28, Pages 19196-19203Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M600166200
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Funding
- NIDDK NIH HHS [DK066428, R01 DK066428] Funding Source: Medline
- NIGMS NIH HHS [T32 GM08492, R01 GM038542-19, R01 GM038542, T32 GM008492] Funding Source: Medline
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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)(6)P 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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