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M208993200v1
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Papers In Press, published online ahead of print November 8, 2002
J. Biol. Chem, 10.1074/jbc.M208993200
Submitted on September 3, 2002
Revised on November 8, 2002
Accepted on November 8, 2002

Nak1, an essential GC kinase regulates cell morphology and growth in Schizosaccharomyces pombe

Timothy Y. Huang, Nancy A. Markley, and Dallan Young

Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N4N1

Corresponding Author: young{at}ucalgary.ca

We have identified and characterized Nak1, a 652 aa N-terminal kinase belonging to the group II GCK family, in Schizosaccharomyces pombe. We found that nak1 is essential for cell proliferation. Furthermore, partial repression of nak1, under regulation of an integrated nmt1 promoter, resulted in an aberrant round cellular morphology, actin and microtubule mislocalization, slow growth, and cell division defects. Overexpression of either a kinase-inactive mutant (Nak1K39R) or the non-catalytic domain resulted in similar phenotypes, suggesting dominant-negative effects. By deletion analysis, we mapped the region responsible for this dominant-negative effect to the C-terminal 99 residues. Furthermore, we found that deletion of the C-terminal 99 residues inhibited Nak1 autophosphorylation, and expression of a partially-inactive (Nak1T171A) or truncated (Nak11-562) protein only weakly suppressed morphological and growth phenotypes, indicating that both kinase and C-terminal regions are important for Nak1 function. GFP-Nak1 localized uniformly throughout the cytoplasm, unlike many other proteins which influence cell polarity that preferentially localize to cell ends. Together, our results implicate Nak1 in the regulation of cell polarity, growth and division, and suggest that the C-terminal end plays an important role in the regulation of this kinase.


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