Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. Signal., 3 January 2012
Vol. 5, Issue 205, p. ec8
[DOI: 10.1126/scisignal.2002808]

EDITORS' CHOICE

Cytoskeleton Mical in Actin Regulation

Stella M. Hurtley

Science, AAAS, Cambridge CB2 1LQ, UK

Cell behavior is controlled by extracellular signals that work through signal transduction pathways to regulate the organization of the actin cytoskeleton. Some of these extrinsic signals positively affect the cytoskeleton and induce actin polymerization, but extrinsic signals that negatively regulate and disassemble actin filaments also exist. A family of multidomain proteins, the MICALs, directly associates with Semaphorins, cell surface receptors involved in negative or repulsive cues. Working with purified proteins and in vivo, Hung et al. now find that actin filaments serve as a direct substrate for Mical's enzymatic activity. Mical posttranslationally alters actin at its methionine 44 residue, which disrupts the association between actin monomers and cutting actin filaments. Altering the methionine 44 residue makes actin resistant to Mical-mediated disassembly in vitro and in vivo in Drosophila.

R.-J. Hung, C. W. Pak, J. R. Terman, Direct redox regulation of F-actin assembly and disassembly by Mical. Science 334, 1710–1713 (2011). [Abstract] [Full Text]

Citation: S. M. Hurtley, Mical in Actin Regulation. Sci. Signal. 5, ec8 (2012).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882