A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation
is inactive as a kinase and relatively long-lived, since the catalytic Nt-domain sterically sequesters C-degron. An induced (e.g., through a regulatory phosphorylation) dissociation of Ct-domain from Nt-domain activates the catalytic Nt-domain and also exposes the C-degron of Chk1. Thus, activation of Chk1 kinase would make it, simultaneously, a short-lived protein.
Authors
- Shun‐Jia Chen (ORCID: https://orcid.org/0000-0002-5489-4930)
- Alexander Varshavsky (ORCID: https://orcid.org/0000-0002-4011-258X)
- Ju-Yeon Hyun (ORCID: https://orcid.org/0000-0002-5526-9651)
- Jang-Hyun Oh
Institutions
- California Institute of Technology (US)
Publication Details
- Journal
- Proceedings of the National Academy of Sciences
- Published
- 2026-04-07
- DOI
- https://doi.org/10.1073/pnas.2605594123
- Primary Topic
- Ubiquitin and proteasome pathways
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institute of General Medical Sciences