This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pendergast, A M Articles by Witte, O N Search for Related Content PubMed PubMed Citation Articles by Pendergast, A M Articles by Witte, O N

Normal cellular and transformation-associated abl proteins share common sites for protein kinase C phosphorylation.

Department of Microbiology, University of California, Los Angeles 90024.

ABSTRACT

Viral transduction and chromosomal translocations of the c-abl gene result in the synthesis of abl proteins with structurally altered amino termini. These altered forms of the abl protein, but not the c-abl proteins, are detectably phosphorylated on tyrosine in vivo. In contrast, all forms of the abl protein are phosphorylated on serine following in vivo labeling with Pi. Treatment of NIH-3T3 cells with protein kinase C activators resulted in a four- to eightfold increase in the phosphorylation of murine c-abl due to modification of two serines on the c-abl protein. Purified protein kinase C phosphorylated all abl proteins at the same two sites. Both sites are precisely conserved in murine and human abl proteins. The sites on the abl proteins were found near the carboxy terminus. In contrast, for the epidermal growth factor receptor (T. Hunter, N. Ling, and J. A. Cooper, Nature [London] 311:480-483, 1984) and pp60src (K. L. Gould, J. R. Woodgett, J. A. Cooper, J. E. Buss, D. Shalloway, and T. Hunter, Cell 42:849-857, 1985), the sites of protein kinase C phosphorylation are amino-terminal to the kinase domain. The abl carboxy-terminal region is not necessary for the tyrosine kinase activity or transformation potential of the viral abl protein and may represent a regulatory domain. Using an in vitro immune complex kinase assay, we were not able to correlate reproducible changes in c-abl activity with phosphorylation by protein kinase C. However, the high degree of conservation of the phosphorylation sites for protein kinase C between human and mouse abl proteins suggests an important functional role.

This article has been cited by other articles:

• Woodring, P. J., Hunter, T., Wang, J. Y. J. (2005). Mitotic Phosphorylation Rescues Abl from F-actin-mediated Inhibition. J. Biol. Chem. 280: 10318-10325 [Abstract] [Full Text]  
• Warren, D., Griffin, D. S., Mainville, C., Rosenberg, N. (2003). The Extreme Carboxyl Terminus of v-Abl Is Required for Lymphoid Cell Transformation by Abelson Virus. J. Virol. 77: 4617-4625 [Abstract] [Full Text]  
• Warren, D., Heilpern, A. J., Berg, K., Rosenberg, N. (2000). The Carboxyl Terminus of v-Abl Protein Can Augment SH2 Domain Function. J. Virol. 74: 4495-4504 [Abstract] [Full Text]  
• Danial, N. N., Losman, J. A., Lu, T., Yip, N., Krishnan, K., Krolewski, J., Goff, S. P., Wang, J. Y. J., Rothman, P. B. (1998). Direct Interaction of Jak1 and v-Abl Is Required for v-Abl-Induced Activation of STATs and Proliferation. Mol. Cell. Biol. 18: 6795-6804 [Abstract] [Full Text]  
• Wen, S.-T., Van Etten, R. A. (1997). The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev. 11: 2456-2467 [Abstract] [Full Text]  
• Dai, Z, Pendergast, A M (1995). Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity.. Genes Dev. 9: 2569-2582 [Abstract]