Arrestin

S-antigen; retina and pineal gland (arrestin)
Struktur kristalografi dari famili bovane arrestin-S.[1]
Pengidentifikasi
SimbolSAG
Simbol alternatifarrestin-1
Gen NCBI6295
HGNC10521
OMIM181031
RefSeqNM_000541
UniProtP10523
Data lain
LokusChr. 2 q37.1
arrestin beta 1
Pengidentifikasi
SimbolARRB1
Simbol alternatifARR1, arrestin-2
Gen NCBI408
HGNC711
OMIM107940
RefSeqNM_004041
UniProtP49407
Data lain
LokusChr. 11 q13
arrestin beta 2
Pengidentifikasi
SimbolARRB2
Simbol alternatifARR2, arrestin-3
Gen NCBI409
HGNC712
OMIM107941
RefSeqNM_004313
UniProtP32121
Data lain
LokusChr. 17 p13
arrestin 3, retinal (X-arrestin)
Pengidentifikasi
SimbolARR3
Simbol alternatifARRX, arrestin-4
Gen NCBI407
HGNC710
OMIM301770
RefSeqNM_004312
UniProtP36575
Data lain
LokusChr. X q

Arrestin (disingkat Arr) adalah famili kecil protein yang penting untuk mengatur transduksi sinyal pada reseptor terhubung protein G.[2][3] Arrestin pertama kali ditemukan sebagai bagian dari mekanisme dua langkah yang dikonservasi untuk mengatur aktivitas reseptor terhubung protein G (GPCR) dalam sistem rhodopsin visual oleh Hermann Kühn, Scott Hall, dan Ursula Wilden[4] dan dalam sistem β-adrenergik oleh Martin J. Lohse dan sejawat.[5][6]

Fungsi

Menanggapi stimulus, GPCR mengaktifkan protein G heterotrimerik. Untuk mematikan respons ini, atau menyesuaikan dengan stimulus yang persisten, reseptor aktif perlu di-desensitasi (dibuat lebih peka). Langkah pertama dalam desensitisasi adalah fosforilasi oleh kelas serin/treonin kinase yang disebut GPCR kinases (GRK). Fosforilasi GRK secara khusus menyiapkan reseptor yang sedang aktif untuk berikatan dengan arrestin. Ikatan arrestin pada reseptor menghambat pensinyalan yang diperantarai protein G lebih lanjut dan menargetkan reseptor untuk internalisasi, dan mengarahkan kembali pensinyalan ke jalur alternatif independen protein G, seperti pensinyalan β-arrestin.[7][8][9][10][6] Selain ke GPCRs, arrestin juga berikatan pada kelas lain dari reseptor permukaan sel dan berbagai protein pensinyalan lainnya.[11]

Subtipe

Arrestin (or S-antigen), N-terminal domain
Structure of arrestin from bovine rod outer segments.[1]
Identifikasi
SimbolArrestin_N
PfamPF00339
Klan PfamCL0135
InterProIPR011021
PROSITEPDOC00267
SCOP1cf1
SUPERFAMILY1cf1
Arrestin (or S-antigen), C-terminal domain
Structure of bovine beta-arrestin.[12]
Identifikasi
SimbolArrestin_C
PfamPF02752
Klan PfamCL0135
InterProIPR011022
SCOP1cf1
SUPERFAMILY1cf1

Referensi

  1. ^ a b PDB: 1CF1​; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (April 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell. 97 (2): 257–69. doi:10.1016/S0092-8674(00)80735-7. PMID 10219246. 
  2. ^ "Regulation of receptor trafficking by GRKs and arrestins". Annual Review of Physiology. 69: 451–82. 2007. doi:10.1146/annurev.physiol.69.022405.154712. PMID 17037978. 
  3. ^ "Transduction of receptor signals by beta-arrestins". Science. 308 (5721): 512–7. April 2005. doi:10.1126/science.1109237. PMID 15845844. 
  4. ^ "Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments". Proceedings of the National Academy of Sciences of the United States of America. 83 (5): 1174–8. March 1986. doi:10.1073/pnas.83.5.1174. PMC 323037 alt=Dapat diakses gratis. PMID 3006038. 
  5. ^ "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962): 1547–50. June 1990. doi:10.1126/science.2163110. PMID 2163110. 
  6. ^ a b "The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics. 110 (3): 465–502. June 2006. doi:10.1016/j.pharmthera.2005.09.008. PMC 2562282 alt=Dapat diakses gratis. PMID 16460808. 
  7. ^ "Biased signalling: from simple switches to allosteric microprocessors". Nature Reviews. Drug Discovery. January 2018. doi:10.1038/nrd.2017.229. PMID 29302067. 
  8. ^ "Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis". Proceedings of the National Academy of Sciences of the United States of America. February 2017. doi:10.1073/pnas.1701529114. PMC 5347553 alt=Dapat diakses gratis. PMID 28223524. 
  9. ^ "Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications. 7: 13416. November 2016. doi:10.1038/ncomms13416. PMC 5105198 alt=Dapat diakses gratis. PMID 27827372. 
  10. ^ "Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation". Molecular Biology of the Cell. 28 (8): 1003–10. April 2017. doi:10.1091/mbc.E16-12-0818. PMC 5391177 alt=Dapat diakses gratis. PMID 28228552. 
  11. ^ "The molecular acrobatics of arrestin activation". Trends in Pharmacological Sciences. 25 (2): 105–11. February 2004. doi:10.1016/j.tips.2003.12.008. PMID 15102497. 
  12. ^ Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (September 2001). "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation". Structure. 9 (9): 869–80. doi:10.1016/S0969-2126(01)00644-X. PMID 11566136. 

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