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Volume 271, Number 44, Issue of November 1, 1996 pp. 27299-27303
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Activity and Autophosphorylation of LAMMER Protein Kinases

(Received for publication, May 10, 1996, and in revised form, September 4, 1996)

Kun Lee , Cheng Du ^¶ , Mark Horn ^¶ and Leonard Rabinow ^¶

From the  Waksman Institute, Rutgers University, Piscataway, New Jersey 08855-0759 and the ^¶ Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska 68198-4525

Clk/STY, the murine homologue of the recently described LAMMER family of protein kinases, autophosphorylates on serine/threonine and tyrosine residues in vitro and in vivo. LAMMER kinases are found throughout eukaryotes and possess virtually complete amino acid identity in many domains critical for kinase function, leading to the question of whether other family members also possess dual specificity. We report here that the Drosophila family member DOA, human SK-G1, and the Saccharomyces cerevisiae KNS1, all possess protein kinase activity and autophosphorylate with dual specificity in vitro, suggesting that the entire family possesses this activity. Although the LAMMER kinases are closely related to the mitogen-activated protein kinase family, they possess different substrate specificity in vitro, based on phosphorylation of peptide and protein substrates and sequencing of a phosphorylation site in a common substrate.

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