Arrestin beta 1 explained

Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.[1] [2]

Function

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.[2] 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.[3]

Interactions

Arrestin beta 1 has been shown to interact with

Further reading

Notes and References

  1. Parruti G, Peracchia F, Sallese M, Ambrosini G, Masini M, Rotilio D, De Blasi A . 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 . May 1993 . 8486659 . 10.1016/S0021-9258(18)98412-7 . free .
  2. Web site: Entrez Gene: ARRB1 arrestin, beta 1.
  3. Peterson YK, Luttrell LM . The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling . Pharmacological Reviews . 69 . 3 . 256–297 . July 2017 . 28626043 . 5482185 . 10.1124/pr.116.013367 .
  4. Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ . beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis . The Journal of Biological Chemistry . 276 . 45 . 42509–42513 . November 2001 . 11533043 . 10.1074/jbc.M108399200 . free .
  5. Conlan LA, Martin TJ, Gillespie MT . The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B . FEBS Letters . 527 . 1–3 . 71–75 . September 2002 . 12220636 . 10.1016/S0014-5793(02)03164-2 . 83640616 . free .
  6. Chen W, Hu LA, Semenov MV, Yanagawa S, Kikuchi A, Lefkowitz RJ, Miller WE . 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 . December 2001 . 11742073 . 64954 . 10.1073/pnas.211572798 . free . 2001PNAS...9814889C .
  7. Wang P, Wu Y, Ge X, Ma L, Pei G . 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 . March 2003 . 12538596 . 10.1074/jbc.M208109200 . free .
  8. Shenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM . Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor . The Journal of Biological Chemistry . 283 . 32 . 22166–22176 . August 2008 . 18544533 . 2494938 . 10.1074/jbc.M709668200 . free .
  9. Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, Ma L, Pei G . 6 . Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor . Journal of Neurochemistry . 76 . 6 . 1887–1894 . March 2001 . 11259507 . 10.1046/j.1471-4159.2001.00204.x . 83485138 . free .
  10. Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS . 6 . Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization . Nature Cell Biology . 4 . 8 . 547–555 . August 2002 . 12105416 . 10.1038/ncb821 . 20784208 .