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Sci. Signal., 14 September 2010
Vol. 3, Issue 139, p. re6
[DOI: 10.1126/scisignal.3139re6]

REVIEWS

ABL Tyrosine Kinases: Evolution of Function, Regulation, and Specificity

John Colicelli*

Department of Biological Chemistry, Molecular Biology Institute and Jonsson Comprehensive Cancer Center, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.

Gloss: ABL-family proteins couple a highly regulated tyrosine kinase domain with an actin-binding and -bundling domain to carry out a set of unique and essential functions. The ABL genes are among the earliest identifiable genes encoding tyrosine kinases, and they show remarkable sequence conservation. Gene duplication produced two vertebrate ABL paralogs with specialized properties. ABL1 evolved nuclear localization signals and a DNA binding domain to mediate damage repair functions. ABL2 developed additional binding domains for actin and microtubules, extending its cytoskeletal remodeling functions. This Review surveys the recent literature and available databases with a focus on ABL evolution and the mechanisms regulating ABL's catalytic activity and substrate specificity. This Review contains 7 figures, 2 tables, and 248 references. A better understanding of these properties could facilitate the design of new treatments for malignancies driven by ABL fusion proteins.

* Corresponding author. Telephone, 310-825-1251; fax, 310-206-1929; e-mail, colicelli{at}mednet.ucla.edu

Citation: J. Colicelli, ABL Tyrosine Kinases: Evolution of Function, Regulation, and Specificity. Sci. Signal. 3, re6 (2010).

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