PA28γ-20S proteasome is a proteolytic complex committed to degrade unfolded proteins.
ATP-independent proteolysis
Intrinsically disordered proteins (IDP)
PA28αβ
PSME 3
Proteasome activator
Proteasome gate
Protein degradation
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
16 Dec 2021
16 Dec 2021
Historique:
received:
06
11
2020
accepted:
17
11
2021
revised:
15
11
2021
pubmed:
17
12
2021
medline:
18
1
2022
entrez:
16
12
2021
Statut:
epublish
Résumé
PA28γ is a nuclear activator of the 20S proteasome that, unlike the 19S regulatory particle, stimulates hydrolysis of several substrates in an ATP- and ubiquitin-independent manner and whose exact biological functions and molecular mechanism of action still remain elusive. In an effort to shed light on these important issues, we investigated the stimulatory effect of PA28γ on the hydrolysis of different fluorogenic peptides and folded or denatured full-length proteins by the 20S proteasome. Importantly, PA28γ was found to dramatically enhance breakdown rates by 20S proteasomes of several naturally or artificially unstructured proteins, but not of their native, folded counterparts. Furthermore, these data were corroborated by experiments in cell lines with a nucleus-tagged myelin basic protein. Finally, mass spectrometry analysis of the products generated during proteasomal degradation of two proteins demonstrated that PA28γ does not increase, but rather decreases, the variability of peptides that are potentially suitable for MHC class I antigen presentation. These unexpected findings indicate that global stimulation of the degradation of unfolded proteins may represent a more general feature of PA28γ and suggests that this proteasomal activator might play a broader role in the pathway of protein degradation than previously believed.
Identifiants
pubmed: 34913092
doi: 10.1007/s00018-021-04045-9
pii: 10.1007/s00018-021-04045-9
doi:
Substances chimiques
Autoantigens
0
Intrinsically Disordered Proteins
0
Ki antigen
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
45Subventions
Organisme : Università degli Studi di Torino
ID : 60% (Ric. Locale)
Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Nature Switzerland AG.
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