A Prenylation Motif Is Required for Plasma-Membrane Localization and Biochemical Function of Casein Kinase-I in Budding Yeast

Vancura, A., Sessler, A., Leichus, B., Kuret, J. (July 1994) A Prenylation Motif Is Required for Plasma-Membrane Localization and Biochemical Function of Casein Kinase-I in Budding Yeast. Journal of Biological Chemistry, 269 (30). pp. 19271-19278. ISSN 0021-9258

URL: http://www.ncbi.nlm.nih.gov/pubmed/8034689

Abstract

The subcellular distribution of three casein kinase I (CK1) homologs, encoded by the YCK1, YCK2, and HRR25 genes, has been determined in budding yeast through a combination of subcellular fractionation and immun ofluorescence methods. Both Yck proteins are tightly associated with the plasma membrane or underlying cytoskeleton and require both high-salt and nonionic detergent for extraction. Association is mediated primarily by the prenylation motif found at the C terminus of both Yck proteins. In contrast, the third CK1 homolog, Hrr25p, is found predominantly in the nucleus and only partially in the plasma membrane. Despite partial colocalization with the Yck proteins, Hrr25p is unable to rescue the yck1 Delta yck2 Delta phenotype. However, a chimeric kinase containing the N-terminal kinase domain of Hrr25p and the C terminal region of Yck2p contains full Yck activity in vivo. These data suggest that members of the casein kinase I family have distinct but partially overlapping distributions in the cell that are mediated by their unique C-terminal regions.

Item Type: Paper
Uncontrolled Keywords: SACCHAROMYCES-CEREVISIAE PROTEIN-KINASE PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE ESSENTIAL COMPONENT NEUROSPORA-CRASSA ADENYLYL CYCLASE BETA-CASEIN CELL CYCLE PHOSPHORYLATION RAS
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Stillman lab
Depositing User: Matt Covey
Date: July 1994
Date Deposited: 03 Aug 2015 19:12
Last Modified: 03 Aug 2015 19:12
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31442

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