Arrestin beta 1

(Redirected from ARRB1)

Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.[5][6]

ARRB1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesARRB1, ARB1, ARR1, Arrestin beta 1
External IDsOMIM: 107940; MGI: 99473; HomoloGene: 2981; GeneCards: ARRB1; OMA:ARRB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004041
NM_020251

NM_177231
NM_178220

RefSeq (protein)

NP_004032
NP_064647

NP_796205
NP_835738

Location (UCSC)Chr 11: 75.26 – 75.35 MbChr 7: 99.18 – 99.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described, however, their exact functions are not known.[6] Beta-arrestin has been shown to play a role as a scaffold that binds intermediates and may direct G-protein signaling by connecting receptors to clathrin-mediated endocytosis.[7]

Interactions

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Arrestin beta 1 has been shown to interact with

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137486Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018909Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Parruti G, Peracchia F, Sallese M, Ambrosini G, Masini M, Rotilio D, De Blasi A (May 1993). "Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing". The Journal of Biological Chemistry. 268 (13): 9753–9761. doi:10.1016/S0021-9258(18)98412-7. PMID 8486659.
  6. ^ a b "Entrez Gene: ARRB1 arrestin, beta 1".
  7. ^ Peterson YK, Luttrell LM (July 2017). "The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling". Pharmacological Reviews. 69 (3): 256–297. doi:10.1124/pr.116.013367. PMC 5482185. PMID 28626043.
  8. ^ a b Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (November 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry. 276 (45): 42509–42513. doi:10.1074/jbc.M108399200. PMID 11533043.
  9. ^ Conlan LA, Martin TJ, Gillespie MT (September 2002). "The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B". FEBS Letters. 527 (1–3): 71–75. doi:10.1016/S0014-5793(02)03164-2. PMID 12220636. S2CID 83640616.
  10. ^ Chen W, Hu LA, Semenov MV, Yanagawa S, Kikuchi A, Lefkowitz RJ, Miller WE (December 2001). "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 14889–14894. Bibcode:2001PNAS...9814889C. doi:10.1073/pnas.211572798. PMC 64954. PMID 11742073.
  11. ^ Wang P, Wu Y, Ge X, Ma L, Pei G (March 2003). "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". The Journal of Biological Chemistry. 278 (13): 11648–11653. doi:10.1074/jbc.M208109200. PMID 12538596.
  12. ^ Shenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM (August 2008). "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". The Journal of Biological Chemistry. 283 (32): 22166–22176. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533.
  13. ^ Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, et al. (March 2001). "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry. 76 (6): 1887–1894. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507. S2CID 83485138.
  14. ^ Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, et al. (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nature Cell Biology. 4 (8): 547–555. doi:10.1038/ncb821. PMID 12105416. S2CID 20784208.

Further reading

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