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A
non-receptor tyrosine kinase of the src family but distinguished from
other members by its large COOH terminal domain. To forms of the
normal protein exist which differ in the extreme N terminal. One
form (type IV/Ib) is myristoylated on the N-terminal glycine, the other
normal form (I/Ia) in not. c-Abl contains both a G-actin binding site
and an independent F-actin site.
References:-
McWhirter,
J.R., Wang, J.Y.J. (1991). "Activation of tyrosine kinase and
microfilament-binding functions of c-abl by bcr sequences
in bcr/abl fusion proteins." Mol.Cell.Biol. 11,
1785-1792.
McWhirter,
J.R., Wang, J.Y.J. (1993). "An actin -binding function contributes
to transformation by the Bcr-Abl oncoprotein of the Philadelphia
chromosome-positive leukemias. EMBO J. 12, 1533-1546.
Van
Etten, R.A., Jackson, P.K., Baltimore, D., Sander, M.C., Matsudaira, P.T.
& Janmey, P.A. (1994). "The COOH terminus of the c-Abl tyrosine
kinase contains distinct F-actin and G-actin binding domains with
bundling activity." J.Cell Biol. 124, 325-340.
Wills, Z., Bateman, J., Korey, C. A., Comer, A.
& Van Vactor, D. (1999) The tyrosine kinase Abl and its substrate
enabled collaborate with the receptor phosphase Dlar to control motor
axon guidance., Neuron. 22, 301-312.
Wills, Z., Marr, L., Zinn, K., Goodman, C. S.
& Van Vactor, D. (1999) Profilin and the Abl tyrosine kinase are
required for motor axon outgrowth in the Drosophila embryo., Neuron.
22, 291-299.
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