Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1.

The Journal of Biological Chemistry
Adam ZwolakNico Tjandra

Abstract

Capping protein (CP) is a ubiquitously expressed, 62-kDa heterodimer that binds the barbed end of the actin filament with approximately 0.1 nm affinity to prevent further monomer addition. CARMIL is a multidomain protein, present from protozoa to mammals, that binds CP and is important for normal actin dynamics in vivo. The CARMIL CP binding site resides in its CAH3 domain (CARMIL homology domain 3) located at or near the protein's C terminus. CAH3 binds CP with approximately 1 nm affinity, resulting in a complex with weak capping activity (30-200 nm). Solution assays and single-molecule imaging show that CAH3 binds CP already present on the barbed end, causing a 300-fold increase in the dissociation rate of CP from the end (i.e. uncapping). Here we used nuclear magnetic resonance (NMR) to define the molecular interaction between the minimal CAH3 domain (CAH3a/b) of mouse CARMIL-1 and CP. Specifically, we show that the highly basic CAH3a subdomain is required for the high affinity interaction of CAH3 with a complementary "acidic groove" on CP opposite its actin-binding surface. This CAH3a-CP interaction orients the CAH3b subdomain, which we show is also required for potent anti-CP activity, directly adjacent to the basic patch ...Continue Reading

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Citations

Sep 28, 2013·Nature Communications·Adam ZwolakRoberto Dominguez
Mar 14, 2012·The Journal of Biological Chemistry·Taekyung KimJohn A Cooper
Apr 30, 2014·Proceedings of the National Academy of Sciences of the United States of America·Ikuko FujiwaraJohn A Hammer
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Feb 28, 2021·Journal of Molecular Biology·Shuichi TakedaYuichiro Maéda

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