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A Cdc42- and Rac-interactive binding (CRIB) domain mediates functions of coronin
Müller-Taubenberger, A. Faix, J. Rivero, F. Noegel, A.A.
Müller-Taubenberger, A.
Faix, J.
Rivero, F.
Noegel, A.A.
Publication Date
2014-01
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© 2013 The Authors. Reproduced in accordance with the publisher's self-archiving policy.
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2013-11-20
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Abstract
The Cdc42- and Rac-interactive binding motif (CRIB) of coronin binds to Rho GTPases with a preference for GDP-loaded Rac. Mutation of the Cdc42- and Rac-interactive binding motif abrogates Rac binding. This results in increased 1evels of activated Rac in coronin-deficient Dictyostelium cells (corA−), which impacts myosin II assembly. corA− cells show increased accumulation of myosin II in the cortex of growth-phase cells. Myosin II assembly is regulated by myosin heavy chain kinase–mediated phosphorylation of its tail. Kinase activity depends on the activation state of the p21-activated kinase a. The myosin II defect of corA− mutant is alleviated by dominant-negative p21-activated kinase a. It is rescued by wild-type coronin, whereas coronin carrying a mutated Cdc42- and Rac-interactive binding motif failed to rescue the myosin defect in corA− mutant cells. Ectopically expressed myosin heavy chain kinases affinity purified from corA− cells show reduced kinase activity. We propose that coronin through its affinity for GDP–Rac regulates the availability of GTP–Rac for activation of downstream effectors.
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Swaminathan K, Müller-Taubenberger A, Faix J et al (2014) A Cdc42- and Rac-interactive binding (CRIB) domain mediates functions of coronin. PNAS: Proceedings of the National Academy of Sciences of the United States of America. 111(1): E25-E33.
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