ARRB1
ARRB1 (Beta-arrestin-1) is a protein that switches other genes on and off. In the public catalogues the evidence so far is association rather than a proven role.
Overview
Functions in regulating agonist-mediated G protein-coupled receptor (GPCR) signalling by mediating both receptor desensitisation and resensitisation processes. During homologous desensitisation, beta-arrestins bind to the GPCR-phosphorylated receptor and sterically preclude its coupling to the cognate G protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalisation by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs).
Open Targets scores its association with cancer at 0.62 (direct and indirect evidence; datatypes literature 0.95, affected pathway 0.97, animal model 0.48, genetic association 0.00).
- Target · the protein and the cell it sits on
- Drug · antibody, small molecule, cell or radioligand
- Effect · signal, damage or kill
In plain words · ARRB1 (Beta-arrestin-1) is a protein that switches other genes on and off. In the public catalogues the evidence so far is association rather than a proven role.
- 1 · What it is
ARRB1 (Beta-arrestin-1) is a protein that switches other genes on and off. In the public catalogues the evidence so far is association rather than a proven role.
- 2 · What goes wrong in cancer
Functions in regulating agonist-mediated G protein-coupled receptor (GPCR) signalling by mediating both receptor desensitisation and resensitisation processes.
- 3 · How drugs use it
No product in this corpus aims at ARRB1 yet. Transcription factors have no pocket to plug, so drugs either degrade them or block the partner protein they need to dock on DNA.
External identifiers
Sources: HGNC HGNC:711 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P49407 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000137486 (association with cancer (MONDO_0004992) 0.62; (GraphQL API, CC0))
Biology
Functions in regulating agonist-mediated G protein-coupled receptor (GPCR) signalling by mediating both receptor desensitisation and resensitisation processes. During homologous desensitisation, beta-arrestins bind to the GPCR-phosphorylated receptor and sterically preclude its coupling to the cognate G protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalisation by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalised arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G proteins. Two different modes of arrestin-mediated internalisation occur. Location: Cytoplasm; Nucleus; Cell membrane; Membrane, clathrin-coated pit (UniProt). Locus 11q13.4 (HGNC).
Notes
top- Written by scripts/fetch-cancer-genes.ts from CIViC, Open Targets, IntOGen, HGNC and UniProt; the function text is UniProt's, condensed and in UK spelling. Roles: none stated by the sources. Evidence tier "association-only" is the strongest of those signals.
- Prevalence not recorded: none of the sources gives a positivity rate.
Latest papers
topQuery for this target: (TITLE:"ARRB1" OR ABSTRACT:"ARRB1" OR TITLE:"arrestin beta 1" OR ABSTRACT:"arrestin beta 1" OR TITLE:"Beta-arrestin-1" OR ABSTRACT:"Beta-arrestin-1" OR TITLE:"ARR1" OR ABSTRACT:"ARR1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about ARRB1, not a curated reading list.