Cpc2, a Fission Yeast Homologue of Mammalian RACK1 Protein, Interacts with Ran1 (Pat1) Kinase To Regulate Cell Cycle Progression and Meiotic Development
| Autor: | Maureen McLeod, Lin Hu, Hua Chen, Wei Wang, Anthony Caporaso, Boris Shor |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Recombinant Fusion Proteins
Genes Fungal Molecular Sequence Data Protein Serine-Threonine Kinases Receptors for Activated C Kinase MAP2K7 Fungal Proteins Two-Hybrid System Techniques Schizosaccharomyces Animals Humans Amino Acid Sequence Kinase activity Protein kinase A Cell Growth and Development Molecular Biology Protein Kinase C Gene Library Cell Nucleus Mammals Cyclin-dependent kinase 1 Sequence Homology Amino Acid biology Cyclin-dependent kinase 4 fungi Cell Cycle Cyclin-dependent kinase 2 Cell Biology biology.organism_classification Cyclic AMP-Dependent Protein Kinases Cell biology Meiosis Schizosaccharomyces pombe biology.protein Schizosaccharomyces pombe Proteins Cyclin-dependent kinase 7 Peptides Protein Kinases |
| Zdroj: | Molecular and Cellular Biology. 20:4016-4027 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.20.11.4016-4027.2000 |
| Popis: | The Schizosaccharomyces pombe ran1/pat1 gene regulates the transition between mitosis and meiosis. Inactivation of Ran1 (Pat1) kinase is necessary and sufficient for cells to exit the cell cycle and undergo meiosis. The yeast two-hybrid interaction trap was used to identify protein partners for Ran1/Pat1. Here we report the identification of one of these, Cpc2. Cpc2 encodes a homologue of RACK1, a WD protein with homology to the beta subunit of heterotrimeric G proteins. RACK1 is a highly conserved protein, although its function remains undefined. In mammalian cells, RACK1 physically associates with some signal transduction proteins, including Src and protein kinase C. Fission yeast cells containing a cpc2 null allele are viable but cell cycle delayed. cpc2Delta cells fail to accumulate in G(1) when starved of nitrogen. This leads to defects in conjugation and meiosis. Copurification studies show that although Cpc2 and Ran1 (Pat1) physically associate, Cpc2 does not alter Ran1 (Pat1) kinase activity in vitro. Using a Ran1 (Pat1) fusion to green fluorescent protein, we show that localization of the kinase is impaired in cpc2Delta cells. Thus, in parallel with the proposed role of RACK1 in mammalian cells, fission yeast cpc2 may function as an anchoring protein for Ran1 (Pat1) kinase. All defects associated with loss of cpc2 are reversed in cells expressing mammalian RACK1, demonstrating that the fission yeast and mammalian gene products are indeed functional homologues. |
| Databáze: | OpenAIRE |
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