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[Cancer Research 63, 873-877, February 15, 2003]
© 2003 American Association for Cancer Research


Molecular Biology and Genetics

Homo- and Hetero-Oligomerization of the c-Abl Kinase and Abelson-Interactor-1

Pang-Dian Fan, Feng Cong and Stephen P. Goff1

Integrated Program in Cellular, Molecular and Biophysical Studies [P-D. F.], Department of Biological Sciences [F. C.], Howard Hughes Medical Institute [S. P. G.], and Department of Biochemistry and Molecular Biophysics [S. P. G.], Columbia University College of Physicians and Surgeons, New York, New York 10032

Oligomerization of the nonreceptor tyrosine kinase c-Abl can activate its transforming potential. Domains mediating oligomerization within the BCR-ABL and TEL-ABL oncoproteins are required for transforming activity, and fusion of inducible dimerization domains to c-Abl can generate chimeric proteins with dimerization-dependent transforming activity. We have found that c-Abl oligomerizes at high levels of expression in COS cells. This interaction is dependent on kinase activity and an intact NH2-terminal region of c-Abl. A binding partner of c-Abl, Abl-interactor-1 (Abi-1), similarly oligomerizes in COS cells. An oligomeric form of Abi-1 interacts with Abl both in vitro and in mammalian cells. These results suggest the possibility that oligomerization of Abl kinases, perhaps involving regulation by their interaction partners, may play a role in modulation of kinase activity in both normal and oncogenic processes.




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Copyright © 2003 by the American Association for Cancer Research.