Autoinhibition of c-Abl.

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Title:	Autoinhibition of c-Abl.
Author(s):	Pluk, W.L.L.P. ; Dorey, K.; Superti-Furga, G.
Publication year:	2002
Source:	Cell, vol. 108, iss. 2, (2002), pp. 247-259
ISSN:	0092-8674
DOI:	https://doi.org/10.1016/S0092-8674(02)00623-2
Publication type:	Article / Letter to editor
Please use this identifier to cite or link to this item : https://hdl.handle.net/2066/186495
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Subject:	Study of abnormal differentiation and transformation processes in heritable and acquired disorders with the use of cell and animal models Bestudering van abnormale differentiatie en transformatieprocessen bij erfelijke of verworven aandoeningen m.b.v. cel- en diermodellen
Organization:	Cell Biology (UMC)
Journal title:	Cell
Volume:	vol. 108
Issue:	iss. 2
Page start:	p. 247
Page end:	p. 259
Abstract:	Despite years of investigation, the molecular mechanism responsible for regulation of the c-Abl tyrosine kinase has remained elusive. We now report inhibition of the catalytic activity of purified c-Abl in vitro, demonstrating that regulation is an intrinsic property of the molecule. We show that the interaction of the N-terminal 80 residues with the rest of the protein mediates autoregulation. This N-terminal "cap" is required to achieve and maintain inhibition, and its loss turns c-Abl into an oncogenic protein and contributes to deregulation of BCR-Abl.