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Volume 270, Number 8, Issue of February 24, 1995 pp. 4066-4075
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Developmental Regulation of Expression and Activity of Multiple Forms of the Drosophila RAC Protein Kinase

(Received for publication, September 9, 1994; and in revised form, November 22, 1994)

Mirjana Andjelkovic ,  Pamela F. Jones ,  Ueli Grossniklaus,  Peter Cron ,  Alexander F. Schier,  Mathias Dick ,  Graeme Bilbe ,  Brian A. Hemmings

We have characterized the Drosophila homologue of the proto-oncogenic RAC protein kinase (DRAC-PK). The DRAC-PK gene gives rise to two transcripts with the same coding potential, generated by the use of two different polyadenylation signals. Each transcript encodes two polypeptides because of the presence of a weaker initiator ACG codon, upstream from the major AUG, such that the larger protein contains an N-terminal extension. Like the human isoforms, DRAC-PKs possess a novel signaling region, the pleckstrin homology domain. DRAC-PK proteins have a similar expression pattern, being regulated both maternally and zygotically, and are expressed throughout Drosophila development. Antisera specific for recombinant DRAC-PK and for its C terminus detected two polypeptides of 66 and 85 kDa in Drosophila extracts. The antirecombinant antisera also recognized a polypeptide of 120 kDa from Drosophila, which apparently shared an epitope related to DRAC-PK sequences. The role of p120 appears to be restricted compared with that of DRAC-PK, since it was not detected in larvae or adult flies. There was no spatial restriction of DRAC-PK expression during embryogenesis, suggesting that localized activation might be a regulatory mechanism for its function. DRAC-PK possesses an intrinsic kinase activity that is 8-fold higher in adult flies than in 0-3-h embryos undergoing rapid mitotic cycles.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.