Nefsky, B., Beach, D. (March 1996) Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of cdc25. Embo J, 15 (6). pp. 1301-12. ISSN 0261-4189 (Print)
Abstract
The level of the mitotic activating tyrosine phosphatase cdc25 is regulated by both transcriptional and post-transcriptional mechanisms in the fission yeast Schizosaccharomyces pombe. We have found that cdc25 is ubiquitinated and have cloned pub1, a gene which regulates this event. Pub1 contains a region highly homologous to the putative catalytic domain of the human protein ubiquitin ligase E6-AP. Disruption of pub1 elevates the level of cdc25 protein in vivo rendering cells relatively resistant to the cdc25-opposing tyrosine kinases wee1 and mik1. In addition, loss of wee1 activity in a pub1-disruption background results in a lethal premature entry into mitosis which can be rescued by loss of cdc25 function. A ubiquitin-thioester adduct of pub1 was isolated from fission yeast and disruption of pub1 dramatically reduced ubiquitination of cdc25 in vivo. These results suggest that pub1 directly ubiquitinates cdc25 in vivo.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Amino Acid Sequence Carbon-Nitrogen Ligases Cell Cycle/ physiology Cell Cycle Proteins/ metabolism Esters/metabolism Fungal Proteins/genetics/ metabolism Gene Expression Regulation, Fungal Ligases/genetics/ metabolism Molecular Sequence Data Nuclear Proteins Phosphoprotein Phosphatase/ metabolism Protein-Tyrosine Kinase/genetics/metabolism RNA Processing, Post-Transcriptional Schizosaccharomyces/genetics/ metabolism Schizosaccharomyces pombe Proteins Sequence Homology, Amino Acid Sulfhydryl Compounds/metabolism Ubiquitins/ metabolism cdc25 Phosphatase |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > ubiquitin ligase |
| CSHL Authors: | |
| Communities: | CSHL labs > Beach lab |
| Depositing User: | Matt Covey |
| Date: | 15 March 1996 |
| Date Deposited: | 22 May 2014 15:59 |
| Last Modified: | 22 May 2014 15:59 |
| PMCID: | PMC450033 |
| URI: | https://repository.cshl.edu/id/eprint/30150 |
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