Functional Mechanisms and Roles of Adaptor Proteins in Abl-Regulated Cytoskeletal Actin Dynamics.pdfVIP

Hindawi Publishing Corporation Journal of Signal Transduction Volume 2012, Article ID 414913, 13 pages doi:10.1155/2012/414913 Review Article Functional Mechanisms and Roles of Adaptor Proteins in Abl-Regulated Cytoskeletal Actin Dynamics Mizuho Sato,1, 2 Masahiro Maruoka,1, 3 and Tatsuo Takeya1 1 Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan 2 Institute of Microbial Diseases, Osaka University, Osaka 565-0871, Japan 3 Laboratory of Single-Molecule Cell Biology, Tohoku University Graduate School of Life Sciences, Aoba-ku, Sendai, Miyagi 980-8578, Japan Correspondence should be addressed to Tatsuo Takeya, ttakeya@bs.naist.jp Received 16 February 2012; Accepted 16 March 2012 Academic Editor: A. Yoshimura Copyright © 2012 Mizuho Sato et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abl is a nonreceptor tyrosine kinase and plays an essential role in the modeling and remodeling of F-actin by transducing extracellular signals. Abl and its paralog, Arg, are unique among the tyrosine kinase family in that they contain an unusual extended C-terminal half consisting of multiple functional domains. This structural characteristic may underlie the role of Abl as a mediator of upstream signals to downstream signaling machineries involved in actin dynamics. Indeed, a group of SH3- containing accessory proteins, or adaptor proteins, have been identified that bind to a proline-rich domain of the C-terminal portion of Abl and modulate its kinase activity, substrate recognition, and intracellular localiz