| Title: |
Protein phosphatase 1: life-course regulation by SDS22 and Inhibitor-3 |
| Authors: |
Cao, Xinyu; Lemaire, Sarah; Bollen, Mathieu |
| Source: |
ISSN:1742-464X ; ISSN:1742-4658 ; Febs Journal, vol. 289 (11), (3072-3085. |
| Publisher Information: |
Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies |
| Publication Year: |
2022 |
| Subject Terms: |
AAA-ATPASE; AURORA B; Biochemistry & Molecular Biology; biogenesis; Cdc48; COMPLEX; GENE; Inhibitor-3; life course; Life Sciences & Biomedicine; mitosis; NUCLEAR-LOCALIZATION; p97; POSITIVE REGULATOR; protein phosphatase 1; Science & Technology; SDS22; SPINDLE; STRUCTURAL BASIS; SUBUNIT; TYPE-1 ACTIVITY; Cdc48/p97; Cell Nucleus; Holoenzymes; Life Change Events; Phosphorylation; 0304 Medicinal and Biomolecular Chemistry; 0601 Biochemistry and Cell Biology; 1101 Medical Biochemistry and Metabolomics; 3101 Biochemistry and cell biology |
| Description: |
Protein phosphatase 1 (PP1) is expressed in all eukaryotic cells and catalyzes a sizable fraction of protein Ser/Thr dephosphorylation events. It is tightly regulated in space and time through association with a wide array of regulatory interactors of protein phosphatase one (RIPPOs). Suppressor-of-Dis2-number 2 (SDS22) and Inhibitor-3 (I3), which form a ternary complex with PP1, are the first two evolved and most widely expressed RIPPOs. Their deletion causes mitotic-arrest phenotypes and is lethal in some organisms. The role of SDS22 and I3 in PP1 regulation has been a mystery for decades as they were independently identified as both activators and inhibitors of PP1. This conundrum has largely been solved by recent reports showing that SDS22 and I3 control multiple steps of the life course of PP1. Indeed, they contribute to (a) the stabilization and activation of newly translated PP1, (b) the translocation of PP1 to the nucleus, and (c) the storage of PP1 as a reserve for holoenzyme assembly. Preliminary evidence suggests that SDS22 and I3 may also function as scavengers of released or aged PP1 for re-use in holoenzyme assembly or proteolytical degradation, respectively. Hence, SDS22 and I3 are emerging as master regulators of the life course of PP1. ; sponsorship: The authors' work related to the life course of PP1 is financially supported by FWO grant G090921N. (FWO|G090921N) ; status: Published |
| Document Type: |
article in journal/newspaper |
| File Description: |
application/pdf |
| Language: |
English |
| Relation: |
https://lirias.kuleuven.be/handle/20.500.12942/705927; https://doi.org/10.1111/febs.16029; https://pubmed.ncbi.nlm.nih.gov/34028981 |
| DOI: |
10.1111/febs.16029 |
| Availability: |
https://lirias.kuleuven.be/handle/20.500.12942/705927; https://hdl.handle.net/20.500.12942/705927; https://lirias.kuleuven.be/retrieve/d36e16b6-1581-4a6d-8daf-3b5296ec86e6; https://doi.org/10.1111/febs.16029; https://pubmed.ncbi.nlm.nih.gov/34028981 |
| Rights: |
info:eu-repo/semantics/openAccess ; public ; All rights reserved |
| Accession Number: |
edsbas.8B3CD6B8 |
| Database: |
BASE |