Receptor for activated C kinase 1

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Available structures
PDB Ortholog search: PDBe RCSB
Aliases RACK1, Gnb2-rs1, H12.3, HLC-7, PIG21, GNB2L1, receptor for activated C kinase 1
External IDs MGI: 101849 HomoloGene: 4446 GeneCards: RACK1
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 5: 181.24 – 181.25 Mb Chr 11: 48.8 – 48.81 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Receptor for activated C kinase 1 (RACK1, also known as guanine nucleotide-binding protein subunit beta-2-like 1 (GNB2L1), is a 32 kDa protein that in humans is encoded by the RACK1 gene.[3][4]


RACK1 has been shown to interact with::

See also[edit]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Ron D, Chen CH, Caldwell J, Jamieson L, Orr E, Mochly-Rosen D (Feb 1994). "Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins". Proceedings of the National Academy of Sciences of the United States of America. 91 (3): 839–43. PMC 521407Freely accessible. PMID 8302854. doi:10.1073/pnas.91.3.839. 
  4. ^ Guillemot F, Billault A, Auffray C (Jun 1989). "Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex". Proceedings of the National Academy of Sciences of the United States of America. 86 (12): 4594–8. PMC 287317Freely accessible. PMID 2499885. doi:10.1073/pnas.86.12.4594. 
  5. ^ Wang W, Huang Y, Zhou Z, Tang R, Zhao W, Zeng L, Xu M, Cheng C, Gu S, Ying K, Xie Y, Mao Y (Jan 2002). "Identification and characterization of AGTRAP, a human homolog of murine Angiotensin II Receptor-Associated Protein (Agtrap)". The International Journal of Biochemistry & Cell Biology. 34 (1): 93–102. PMID 11733189. doi:10.1016/s1357-2725(01)00094-2. 
  6. ^ Rigas AC, Ozanne DM, Neal DE, Robson CN (Nov 2003). "The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway". The Journal of Biological Chemistry. 278 (46): 46087–93. PMID 12958311. doi:10.1074/jbc.M306219200. 
  7. ^ a b Liliental J, Chang DD (Jan 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". The Journal of Biological Chemistry. 273 (4): 2379–83. PMID 9442085. doi:10.1074/jbc.273.4.2379. 
  8. ^ Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM (Nov 2002). "Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction". Osteoarthritis and Cartilage / OARS, Osteoarthritis Research Society. 10 (11): 890–7. PMID 12435334. doi:10.1053/joca.2002.0842. 
  9. ^ Diederichs S, Bäumer N, Ji P, Metzelder SK, Idos GE, Cauvet T, Wang W, Möller M, Pierschalski S, Gromoll J, Schrader MG, Koeffler HP, Berdel WE, Serve H, Müller-Tidow C (Aug 2004). "Identification of interaction partners and substrates of the cyclin A1-CDK2 complex". The Journal of Biological Chemistry. 279 (32): 33727–41. PMID 15159402. doi:10.1074/jbc.M401708200. 
  10. ^ Ceci M, Gaviraghi C, Gorrini C, Sala LA, Offenhäuser N, Marchisio PC, Biffo S (Dec 2003). "Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly". Nature. 426 (6966): 579–84. PMID 14654845. doi:10.1038/nature02160. 
  11. ^ Yaka R, He DY, Phamluong K, Ron D (Mar 2003). "Pituitary adenylate cyclase-activating polypeptide (PACAP(1-38)) enhances N-methyl-D-aspartate receptor function and brain-derived neurotrophic factor expression via RACK1". The Journal of Biological Chemistry. 278 (11): 9630–8. PMID 12524444. doi:10.1074/jbc.M209141200. 
  12. ^ Yaka R, Thornton C, Vagts AJ, Phamluong K, Bonci A, Ron D (Apr 2002). "NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5710–5. PMC 122836Freely accessible. PMID 11943848. doi:10.1073/pnas.062046299. 
  13. ^ a b Usacheva A, Smith R, Minshall R, Baida G, Seng S, Croze E, Colamonici O (Jun 2001). "The WD motif-containing protein receptor for activated protein kinase C (RACK1) is required for recruitment and activation of signal transducer and activator of transcription 1 through the type I interferon receptor". The Journal of Biological Chemistry. 276 (25): 22948–53. PMID 11301323. doi:10.1074/jbc.M100087200. 
  14. ^ Croze E, Usacheva A, Asarnow D, Minshall RD, Perez HD, Colamonici O (Nov 2000). "Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor". Journal of Immunology. 165 (9): 5127–32. PMID 11046044. doi:10.4049/jimmunol.165.9.5127. 
  15. ^ a b c Usacheva A, Tian X, Sandoval R, Salvi D, Levy D, Colamonici OR (Sep 2003). "The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex". Journal of Immunology. 171 (6): 2989–94. PMID 12960323. doi:10.4049/jimmunol.171.6.2989. 
  16. ^ Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM (Mar 2009). "Structural basis and specificity of human otubain 1-mediated deubiquitination". The Biochemical Journal. 418 (2): 379–90. PMID 18954305. doi:10.1042/BJ20081318. 
  17. ^ Ozaki T, Watanabe K, Nakagawa T, Miyazaki K, Takahashi M, Nakagawara A (May 2003). "Function of p73, not of p53, is inhibited by the physical interaction with RACK1 and its inhibitory effect is counteracted by pRB". Oncogene. 22 (21): 3231–42. PMID 12761493. doi:10.1038/sj.onc.1206382. 
  18. ^ Yarwood SJ, Steele MR, Scotland G, Houslay MD, Bolger GB (May 1999). "The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform". The Journal of Biological Chemistry. 274 (21): 14909–17. PMID 10329691. doi:10.1074/jbc.274.21.14909. 
  19. ^ Steele MR, McCahill A, Thompson DS, MacKenzie C, Isaacs NW, Houslay MD, Bolger GB (Jul 2001). "Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5". Cellular Signalling. 13 (7): 507–13. PMID 11516626. doi:10.1016/s0898-6568(01)00167-x. 
  20. ^ Ron D, Jiang Z, Yao L, Vagts A, Diamond I, Gordon A (Sep 1999). "Coordinated movement of RACK1 with activated betaIIPKC". The Journal of Biological Chemistry. 274 (38): 27039–46. PMID 10480917. doi:10.1074/jbc.274.38.27039. 
  21. ^ Liedtke CM, Yun CH, Kyle N, Wang D (Jun 2002). "Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor". The Journal of Biological Chemistry. 277 (25): 22925–33. PMID 11956211. doi:10.1074/jbc.M201917200. 
  22. ^ Hellberg CB, Burden-Gulley SM, Pietz GE, Brady-Kalnay SM (Mar 2002). "Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells". The Journal of Biological Chemistry. 277 (13): 11165–73. PMID 11801604. doi:10.1074/jbc.M112157200. 
  23. ^ Mourton T, Hellberg CB, Burden-Gulley SM, Hinman J, Rhee A, Brady-Kalnay SM (May 2001). "The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts". The Journal of Biological Chemistry. 276 (18): 14896–901. PMID 11278757. doi:10.1074/jbc.M010823200. 
  24. ^ Koehler JA, Moran MF (May 2001). "RACK1, a protein kinase C scaffolding protein, interacts with the PH domain of p120GAP". Biochemical and Biophysical Research Communications. 283 (4): 888–95. PMID 11350068. doi:10.1006/bbrc.2001.4889. 
  25. ^ Battle MA, Maher VM, McCormick JJ (Jun 2003). "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways". Biochemistry. 42 (24): 7270–82. PMID 12809483. doi:10.1021/bi034081y. 
  26. ^ Chang BY, Conroy KB, Machleder EM, Cartwright CA (Jun 1998). "RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells". Molecular and Cellular Biology. 18 (6): 3245–56. PMC 108906Freely accessible. PMID 9584165. doi:10.1128/mcb.18.6.3245. 

Further reading[edit]