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Deregulated activity of the Abl protein tyrosine kinase is oncogenic in humans and in animals. The normal cellular form of the enzyme is maintained at a low state of activity by mechanisms that have not yet been entirely elucidated. In particular, little is known about the  trans -acting cellular factors involved. We have tested the activity of human c-Abl microinjected into oocytes of  Xenopus laevis . In contrast to versions of Abl capable of transforming mammalian cells, which were highly active when introduced into oocytes, the activity of wild type c-Abl was inhibited. Oncogenic forms of Abl efficiently enhanced the ability of  Xenopus  oocytes to enter M phase following stimulation by progesterone. Abl-enhanced maturation was normal as judged by accumulation of Mos as well as activation of MAP kinase and Cdc2/CyclinB (MPF). Concomitant with maturation and activation of these kinases, Abl became extensively phosphorylated. Altogether, this suggests that an SH3 domain-dependent Abl regulation mechanism similar to the one observed in mammalian cells operates in  Xenopus  oocytes. Maturation enhancement by microinjection into  Xenopus  oocytes represents a useful novel assay for analyzing Abl activity. Moreover, the  Xenopus  oocyte may be a convenient source of  trans -acting Abl regulators for biochemical studies.

biological chemistry

Regulation of Human c-Abl Tyrosine Kinase Activity in &lt;I&gt;Xenopus&lt;/I&gt; Oocytes and Acceleration of Progesterone-Induced G2/M Transition by Oncogenic Forms