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J. Biol. Chem., Vol. 278, Issue 2, 991-997, January 10, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/2/991    most recent M208993200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Huang, T. Y. Articles by Young, D. Search for Related Content PubMed PubMed Citation Articles by Huang, T. Y. Articles by Young, D. Social Bookmarking                      What's this?

Nak1, an Essential Germinal Center (GC) Kinase Regulates Cell Morphology and Growth in Schizosaccharomyces pombe^*

Timothy Y. Huang, Nancy A. Markley^§, and Dallan Young^¶

From the Department of Biochemistry & Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada

We have identified and characterized Nak1, a 652- amino acid NH₂-terminal kinase belonging to the group II germinal center kinase (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 (Nak1^K39R) 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 COOH-terminal 99 residues. Furthermore, we found that deletion of the COOH-terminal 99 residues inhibited Nak1 autophosphorylation, and expression of a partially inactive (Nak1^T171A) or truncated (Nak1^1-562) protein only weakly suppressed morphological and growth phenotypes, indicating that both kinase and COOH-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 COOH-terminal end plays an important role in the regulation of this kinase.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF091345.

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