The RNA-binding protein HuR is a novel target of Pirh2 E3 ubiquitin ligase.
Journal
Cell death & disease
ISSN: 2041-4889
Titre abrégé: Cell Death Dis
Pays: England
ID NLM: 101524092
Informations de publication
Date de publication:
05 06 2021
05 06 2021
Historique:
received:
05
01
2021
accepted:
24
05
2021
revised:
18
05
2021
entrez:
6
6
2021
pubmed:
7
6
2021
medline:
14
10
2021
Statut:
epublish
Résumé
The RING-finger protein Pirh2 is a p53 family-specific E3 ubiquitin ligase. Pirh2 also ubiquitinates several other important cellular factors and is involved in carcinogenesis. However, its functional role in other cellular processes is poorly understood. To address this question, we performed a proteomic search for novel interacting partners of Pirh2. Using the GST-pulldown approach combined with LC-MS/MS, we revealed 225 proteins that interacted with Pirh2. We found that, according to the GO description, a large group of Pirh2-associated proteins belonged to the RNA metabolism group. Importantly, one of the identified proteins from that group was an RNA-binding protein ELAVL1 (HuR), which is involved in the regulation of splicing and protein stability of several oncogenic proteins. We demonstrated that Pirh2 ubiquitinated the HuR protein facilitating its proteasome-mediated degradation in cells. Importantly, the Pirh2-mediated degradation of HuR occurred in response to heat shock, thereby affecting the survival rate of HeLa cells under elevated temperature. Functionally, Pirh2-mediated degradation of HuR augmented the level of c-Myc expression, whose RNA level is otherwise attenuated by HuR. Taken together, our data indicate that HuR is a new target of Pirh2 and this functional interaction contributes to the heat-shock response of cancer cells affecting their survival.
Identifiants
pubmed: 34091597
doi: 10.1038/s41419-021-03871-w
pii: 10.1038/s41419-021-03871-w
pmc: PMC8179929
doi:
Substances chimiques
ELAV-Like Protein 1
0
ELAVL1 protein, human
0
RNA-Binding Proteins
0
RCHY1 protein, human
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
581Subventions
Organisme : Russian Foundation for Basic Research (RFBR)
ID : 18-29-09144
Organisme : Russian Foundation for Basic Research (RFBR)
ID : 18-29-09144
Organisme : Russian Science Foundation (RSF)
ID : 18-75-10076
Organisme : Russian Science Foundation (RSF)
ID : 18-75-10076
Organisme : Russian Science Foundation (RSF)
ID : 18-75-10076
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