Arrestin beta 2

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Protein-coding gene in the species Homo sapiens

title: "Arrestin beta 2" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["genes", "human-proteins"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/genes" source: "https://en.wikipedia.org/wiki/Arrestin_beta_2" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Beta-arrestin-2, or β-arrestin2, also known as arrestin beta-2, is an intracellular protein that in humans is encoded by the ARRB2 gene.

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, as well as having signalling roles in their own right. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.

The protein may interact with the agonist DOI in 5-HT2A receptor signaling.

Arrestin beta 2 is crucial for the development of tolerance to morphine and other opioids.

Interactions

Arrestin beta 2 has been shown to interact with

References

References

  1. (July 2008). "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology.
  2. (March 2009). "Improvement of morphine-mediated analgesia by inhibition of β-arrestin2 expression in mice periaqueductal gray matter". International Journal of Molecular Sciences.
  3. (January 2008). "Beta-arrestin-dependent mu-opioid receptor-activated extracellular signal-regulated kinases (ERKs) Translocate to Nucleus in Contrast to G protein-dependent ERK activation". Molecular Pharmacology.
  4. (January 2007). "Beta-arrestin signaling and regulation of transcription". Journal of Cell Science.
  5. (March 2008). "Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction". British Journal of Pharmacology.
  6. (February 2008). "Beta-arrestins: multifunctional cellular mediators". Physiology.
  7. (March 2009). "Physiologic and cardiac roles of beta-arrestins". Journal of Molecular and Cellular Cardiology.
  8. (2009). "Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions". Current Pharmaceutical Design.
  9. "ARRB2 arrestin beta 2 [ Homo sapiens (human) ]". [[National Center for Biotechnology Information]].
  10. (January 2008). "Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo". Proceedings of the National Academy of Sciences of the United States of America.
  11. (January 2008). "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America.
  12. (March 1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proceedings of the National Academy of Sciences of the United States of America.
  13. (August 2002). "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking". The Journal of Biological Chemistry.
  14. (November 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry.
  15. (February 2003). "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". The Journal of Biological Chemistry.
  16. (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.
  17. (August 2008). "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". The Journal of Biological Chemistry.
  18. (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nature Cell Biology.

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