Reference - PMID:8635463 - Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of cdc25.
Reference summary
- PubMed ID
- PMID:8635463
- Title
- Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of cdc25.
- Authors
- Nefsky B, Beach D
- Citation
- EMBO J 1996 Mar 15;15(6):1301-12
- Publication year
- 1996
- 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.
