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Volume 270, Number 37, Issue of September 15, pp. 21524-21531, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Alternative Splicing of STY, a Nuclear Dual Specificity Kinase

(Received for publication, February 22, 1995; and in revised form, June 20, 1995)

Peter I. Duncan Brian W. Howell Ricardo M. Marius Suzana Drmanic Elizabeth M. J. Douville John C. Bell

The LAMMER subfamily of kinases has been conserved throughout evolution, and its members are thought to play important roles in the regulation of cellular growth and differentiation programs. STY is a murine LAMMER kinase which has been implicated in the control of PC12 cell differentiation. Multiple transcripts are derived from the Sty gene, and their relative abundance is developmentally regulated. Alternative splicing of the primary Sty transcript generates mRNAs encoding full-length catalytically active (STY) and truncated, kinase-deficient polypeptides. Both STY and its truncated isoform, STY^T, are localized in the nucleus and are capable of heterodimerizing. We also demonstrate that STY functions as a dual specificity kinase in mammalian cells.




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