Cdc48 influence on separase levels is independent of mitosis and suggests translational sensitivity of separase.
Cell Rep
; 38(12): 110554, 2022 03 22.
Article
in En
| MEDLINE
| ID: mdl-35320724
ABSTRACT
Cdc48 (p97/VCP) is a AAA-ATPase that can extract ubiquitinated proteins from their binding partners and can cooperate with the proteasome for their degradation. A fission yeast cdc48 mutant (cdc48-353) shows low levels of the cohesin protease, separase, and pronounced chromosome segregation defects in mitosis. Separase initiates chromosome segregation when its binding partner securin is ubiquitinated and degraded. The low separase levels in the cdc48-353 mutant have been attributed to a failure to extract ubiquitinated securin from separase, resulting in co-degradation of separase along with securin. If true, Cdc48 would be important in mitosis. In contrast, we show here that low separase levels in the cdc48-353 mutant are independent of mitosis. Moreover, we find no evidence of enhanced separase degradation in the mutant. Instead, we suggest that the cdc48-353 mutant uncovers specific requirements for separase translation. Our results highlight a need to better understand how this key mitotic enzyme is synthesized.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Schizosaccharomyces
/
Schizosaccharomyces pombe Proteins
/
Valosin Containing Protein
Type of study:
Diagnostic_studies
Language:
En
Journal:
Cell Rep
Year:
2022
Document type:
Article
Affiliation country:
Estados Unidos