IMR Press / FBL / Volume 7 / Issue 4 / DOI: 10.2741/A767

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article
Abl: mechanisms of regulation and activation
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1 Department of Genetics and Developmental Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3301, USA
2 Program in Biological and Biomedical Sciences, Division of Medical Sciences, Harvard Medical School, Boston, MA 02115, USA
Front. Biosci. (Landmark Ed) 2002, 7(4), 31–42; https://doi.org/10.2741/A767
Published: 1 January 2002
Abstract

The Abl non-receptor tyrosine kinase has been implicated in a wide variety of cellular processes, yet its function and regulation remain poorly understood. Abl has resisted complete understanding not due to lack of interest, but due to the complexity of its overall structure and the corresponding complexity and diversity of its biological activities in the cell. Although Abl consists of many familiar modules with well-understood activities, the ways in which these modules interact are manifold and defy simple categorization. A picture now emerges in which Abl can be potentially regulated in many ways: by phosphorylation, by intramolecular interaction, by interaction with a variety of other proteins, by subcellular localization. Far from being a simple on-off switch, it appears that Abl is better understood as existing in a complex and dynamic equilibrium of states, an equilibrium that can be affected by many signaling inputs. In this review we will discuss the various ways in which the kinase activity of Abl can be regulated; other recent reviews have discussed the larger issue of possible biological roles of Abl (1-3).

Keywords
Protein Tyrosine Kinase
SH2 and SH3 Domains
Phosphorylation
Review
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