ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates in a cytoprotective pathway
| Autor: | Antonis S. Zervos, Lucia Cilenti, Camilla T. Ambivero |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Scaffold protein
BRCC36 isopeptidase (BRISC) complex Cytoplasm Proto-Oncogene Proteins c-jun Protein subunit Molecular Sequence Data Activating transcription factor Kidney Antiviral Agents Deubiquitinating enzyme Protein–protein interaction Activator protein-1 (AP-1) transcription factor Mediator Nuclear Matrix-Associated Proteins Two-Hybrid System Techniques Humans Amino Acid Sequence Abraxas brother 1 (Abro1/KIAA0157) Molecular Biology Transcription factor Cells Cultured Cell Nucleus Genetics Sequence Homology Amino Acid biology Tunicamycin ATF4 Ubiquitination Activating transcription factor 4 (ATF4) Cell Biology Activating Transcription Factor 4 Activating Transcription Factors Cell biology Cytoprotection biology.protein Ubiquitin-Specific Proteases Subcellular Fractions |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. (12):2149-2156 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2012.08.020 |
| Popis: | Abro1 (Abraxas brother 1), also known as KIAA0157, is a scaffold protein that recruits various polypeptides to assemble the BRISC (BRCC36 isopeptide) deubiquitinating enzyme (DUB) complex. The BRISC enzyme has a Lys63-linked deubiquitinating activity and is comprised of four known subunits: MERIT40 (mediator of Rap80 interactions and targeting 40 kDa), BRE (brain and reproductive organ-expressed), BRCC36 (BRCA1/BRCA2-containing complex, subunit 3) and Abro1. We have previously shown that Abro1 has a cytoprotective role that involves the BRISC DUB complex acting on specific Lys63-linked polyubiquitinated substrates. In this report we identify three members of the AP-1 (activating protein-1) family, the ATF4, ATF5 (activating transcription factor) and JunD proteins, as specific interactors of Abro1. The function of ATF4–Abro1 interaction was investigated under normal conditions as well as under cellular stress. Abro1 is predominantly cytoplasmic, but during cellular stress it enters the nucleus and co-localizes with ATF4. Furthermore, this interaction with ATF4 is necessary and essential for the cytoprotective function of Abro1 following oxidative stress. The ability of Abro1 to specifically interact with a number of transcription factors suggests a new mechanism of regulation of the BRISC DUB complex. This regulation involves the participation of at least three known members of the AP-1 family of transcription factors. |
| Databáze: | OpenAIRE |
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