This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Plyte, S. E. Articles by Gould, K. L. Search for Related Content PubMed PubMed Citation Articles by Plyte, S. E. Articles by Gould, K. L.

 Previous Article  |  Next Article 

Mol. Cell. Biol., Jan 1996, 179-191, Vol 16, No. 1
Copyright © 1996, American Society for Microbiology

Schizosaccharomyces pombe skp1+ encodes a protein kinase related to mammalian glycogen synthase kinase 3 and complements a cdc14 cytokinesis mutant [published erratum appears in Mol Cell Biol 1997 Mar;17(3):1756]

SE Plyte, A Feoktistova, JD Burke, JR Woodgett and KL Gould
Ontario Cancer Institute, Toronto, Canada.

We report the cloning of the skp1+ gene, a Schizosaccharomyces pombe homolog of the glycogen synthase kinase 3 (GSK-3) family whose members in higher eukaryotes are involved in cell fate determination, nuclear signalling, and hormonal regulation. skp1 is 67% identical to mammalian GSK-3 beta and displays similar biochemical properties in vitro. Like GSK-3 beta, skp1 is phosphorylated on a conserved tyrosine residue, and this phosphorylation is required for efficient activity. skp1 is also phosphorylated at a serine which has been identified as S-335. Phosphorylation at this site is likely to inhibit its function. Unlike the mammalian enzyme, skp1 both tyrosine autophosphorylates in yeast cells and can phosphorylate other proteins on tyrosine in bacteria. The skp1+ gene is not essential. However, cells with deletions in skp1+ are sensitive to heat shock and exhibit defects in sporulation. Overexpression of wild-type skp1+ specifically complements cdc14-118, one of several mutations causing a defect in cytokinesis. In addition, certain phosphorylation site mutants induce a delay or block in cytokinesis when overexpressed. Together, these data identify novel interactions of a fission yeast GSK-3 homolog with elements of the cytokinesis machinery.

This article has been cited by other articles:

• Bimbo, A., Jia, Y., Poh, S. L., Karuturi, R. K. M., den Elzen, N., Peng, X., Zheng, L., O'Connell, M., Liu, E. T., Balasubramanian, M. K., Liu, J. (2005). Systematic Deletion Analysis of Fission Yeast Protein Kinases. Eukaryot Cell 4: 799-813 [Abstract] [Full Text]  
• Firon, A., Villalba, F., Beffa, R., d'Enfert, C. (2003). Identification of Essential Genes in the Human Fungal Pathogen Aspergillus fumigatus by Transposon Mutagenesis. Eukaryot Cell 2: 247-255 [Abstract] [Full Text]  
• Tanji, C., Yamamoto, H., Yorioka, N., Kohno, N., Kikuchi, K., Kikuchi, A. (2002). A-Kinase Anchoring Protein AKAP220 Binds to Glycogen Synthase Kinase-3beta (GSK-3beta ) and Mediates Protein Kinase A-dependent Inhibition of GSK-3beta. J. Biol. Chem. 277: 36955-36961 [Abstract] [Full Text]  
• Woodgett, J. R. (2001). Judging a Protein by More Than Its Name: GSK-3. Sci Signal 2001: re12-re12 [Abstract] [Full Text]  
• Andoh, T., Hirata, Y., Kikuchi, A. (2000). Yeast Glycogen Synthase Kinase 3 Is Involved in Protein Degradation in Cooperation with Bul1, Bul2, and Rsp5. Mol. Cell. Biol. 20: 6712-6720 [Abstract] [Full Text]  
• Jonak, C., Beisteiner, D., Beyerly, J., Hirt, H. (2000). Wound-Induced Expression and Activation of WIG, a Novel Glycogen Synthase Kinase 3. Plant Cell 12: 1467-1476 [Abstract] [Full Text]  
• Hoyos, M. E., Zhang, S. (2000). Calcium-Independent Activation of Salicylic Acid-Induced Protein Kinase and a 40-Kilodalton Protein Kinase by Hyperosmotic Stress. Plant Physiol. 122: 1355-1364 [Abstract] [Full Text]  
• Balasubramanian, M. K., McCollum, D., Chang, L., Wong, K. C. Y., Naqvi, N. I., He, X., Sazer, S., Gould, K. L. (1998). Isolation and Characterization of New Fission Yeast Cytokinesis Mutants. Genetics 149: 1265-1275 [Abstract] [Full Text]  
• Rogatsky, I., Waase, C. L. M., Garabedian, M. J. (1998). Phosphorylation and Inhibition of Rat Glucocorticoid Receptor Transcriptional Activation by Glycogen Synthase Kinase-3 (GSK-3). SPECIES-SPECIFIC DIFFERENCES BETWEEN HUMAN AND RAT GLUCOCORTICOID RECEPTOR SIGNALING AS REVEALED THROUGH GSK-3 PHOSPHORYLATION. J. Biol. Chem. 273: 14315-14321 [Abstract] [Full Text]  
• Hagan, I, Yanagida, M (1997). Evidence for cell cycle-specific, spindle pole body-mediated, nuclear positioning in the fission yeast Schizosaccharomyces pombe. J. Cell Sci. 110: 1851-1866 [Abstract]