The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

GNB2L1  -  guanine nucleotide binding protein (G...

Homo sapiens

Synonyms: Cell proliferation-inducing gene 21 protein, Gnb2-rs1, Guanine nucleotide-binding protein subunit beta-2-like 1, Guanine nucleotide-binding protein subunit beta-like protein 12.3, H12.3, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of GNB2L1

  • We also show that down-regulation of RACK1 by short interfering RNA inhibits growth and stimulates prostate-specific antigen transcription in androgen-treated prostate cancer cells [1].
  • PDE4D5 and RACK1 interacted with high affinity (Ka approximately 7 nM) [corrected] when they were expressed and purified from Escherichia coli, demonstrating that the interaction does not require intermediate proteins [2].
  • We demonstrate that RACK1 interacts with PTPmu when co-expressed in a recombinant baculovirus expression system [3].
  • 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 [4].
  • Furthermore, RACK1 interacted with mumps virus V protein with a higher affinity than STAT-1 did [5].
  • The significance of this work lies in the discovery of a mechanism by which the growth of colon cancer cells can be slowed, by RACK1 suppression of an oncogenic kinase at critical cell cycle checkpoints [6].
 

Psychiatry related information on GNB2L1

  • Increased association of brain protein kinase C with the receptor for activated C kinase-1 (RACK1) in bipolar affective disorder [7].
  • Moreover, human studies have shown that PKC and its adaptor protein RACK1 are also interdependent in pathological brain aging (e.g., Alzheimer's disease); in fact, calcium-dependent PKC translocation and RACK1 levels are both deficient in an area-selective manner [8].
  • This study examined whether dyslexic children learning to read German show the same nonword reading deficit, which is characteristic of dyslexic children learning to read English (Rack, Olson, & Snowling, 1992), a deficit which is taken as evidence for a phonological impairment underlying dyslexia [9].
 

High impact information on GNB2L1

  • RACK1 competes with HSP90 for binding to the PAS-A domain of HIF-1alpha in vitro and in human cells [10].
  • In finding the role of RACK1 in activation of JNK by PKC, our study also highlights the nature of crosstalk between these two signal-transduction pathways [11].
  • Forced expression of RACK1, which is the plectin-binding receptor protein for activated PKCdelta, in wild-type keratinocytes elevated their migration potential close to that of plectin-null cells [12].
  • MURF1 interacts with receptor for activated protein kinase C (RACK1) and colocalizes with RACK1 after activation with phenylephrine or PMA [13].
  • Consistent with these data, PKCalpha along with the PKC binding protein RACK1 are immunoprecipitated with wild-type P0, and inhibition of PKC activity abolishes P0-mediated adhesion [14].
 

Chemical compound and disease context of GNB2L1

 

Biological context of GNB2L1

  • During a large-scale screen of a human fetal brain cDNA library, a novel human gene GNB2L1 encoding a novel RACK (receptor of activated protein kinase C) protein was isolated and sequenced [15].
  • We also observed RACK1 to suppress ligand-dependent and -independent AR transactivation through PKC activation [16].
  • We show here sequestering of receptor for activated C kinase 1 (RACK1) to the cytoskeleton through the cytoskeletal linker protein plectin during the initial stages of cell adhesion [17].
  • Our results also demonstrate binding of NHERF to RACK1 at the WD5 repeat, which is distinct from the PKCepsilon binding site on the WD6 repeat of RACK1 [18].
  • PKC stimulation led to eIF6 phosphorylation, and mutation of a serine residue in the carboxy terminus of eIF6 impaired RACK1/PKC-mediated translational rescue [19].
 

Anatomical context of GNB2L1

 

Associations of GNB2L1 with chemical compounds

  • Tyrosine phosphorylation on many cellular proteins decreased in 293T cells that transiently overexpressed RACK1 [23].
  • We provide novel evidence that the scaffolding protein RACK1 mediates the interaction between integrin beta chain and activated PKCepsilon [24].
  • UV/DECA treatment of synthetic peptides modeled after the RACK-1-binding site in the C2 region of PKC beta induced modification of Ser218-Leu-Asn-Pro-Glu-Trp-Asn-Glu-Thr226, but not of a control peptide [25].
  • The WD-repeat protein receptor for activated C-kinase (RACK1) was identified by its interaction with the cyclic AMP-specific phosphodiesterase (PDE4) isoform PDE4D5 in a yeast two-hybrid screen [2].
  • Photoinduced inactivation of protein kinase C by dequalinium identifies the RACK-1-binding domain as a recognition site [25].
  • Taken together, the data demonstrate that Tyr-302 in RACK1 is required for interaction with PP2A and beta1 integrin, for regulation of PP2A activity, and for IGF-I-mediated cell migration and proliferation [26].
 

Physical interactions of GNB2L1

  • The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway [16].
  • Furthermore, eIF6 interacts in the cytoplasm with RACK1, a receptor for activated protein kinase C (PKC) [19].
  • In a cytokine signaling cascade, Rack-1 has been reported to interact with the IFN-alphabeta receptor and Stat1 [27].
  • RACK1 also interacted with the IGF-1R in fibroblasts and MCF-7 cells and with endogenous insulin receptor in COS cells [28].
  • Rack-1 interacts weakly with the kinase domain and interacts strongly with the pseudokinase domain of Tyk2 [27].
 

Regulatory relationships of GNB2L1

 

Other interactions of GNB2L1

  • In this report we found that RACK1, which was previously shown to be a protein kinase C (PKC)-anchoring protein that determines the localization of activated PKCbetaII isoform, facilitates ligand-independent AR nuclear translocation upon PKC activation by indolactam V [16].
  • In the IFN system, RACK-1 functions as an adaptor recruiting the transcription factor STAT1 to the receptor complex [34].
  • The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex [34].
  • Finally, we provide evidence that RACK-1 may also serve as a scaffold protein in other cytokine systems such as IL-2, IL-4, and erythropoietin [34].
  • We propose that eIF6 release regulates subunit joining, and that RACK1 provides a physical and functional link between PKC signalling and ribosome activation [19].
 

Analytical, diagnostic and therapeutic context of GNB2L1

References

  1. Receptor for Activated C Kinase 1 (RACK1) and Src Regulate the Tyrosine Phosphorylation and Function of the Androgen Receptor. Kraus, S., Gioeli, D., Vomastek, T., Gordon, V., Weber, M.J. Cancer Res. (2006) [Pubmed]
  2. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. Yarwood, S.J., Steele, M.R., Scotland, G., Houslay, M.D., Bolger, G.B. J. Biol. Chem. (1999) [Pubmed]
  3. The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts. Mourton, T., Hellberg, C.B., Burden-Gulley, S.M., Hinman, J., Rhee, A., Brady-Kalnay, S.M. J. Biol. Chem. (2001) [Pubmed]
  4. 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. Liedtke, C.M., Yun, C.H., Kyle, N., Wang, D. J. Biol. Chem. (2002) [Pubmed]
  5. Association of mumps virus V protein with RACK1 results in dissociation of STAT-1 from the alpha interferon receptor complex. Kubota, T., Yokosawa, N., Yokota, S., Fujii, N. J. Virol. (2002) [Pubmed]
  6. RACK1 inhibits colonic cell growth by regulating Src activity at cell cycle checkpoints. Mamidipudi, V., Dhillon, N.K., Parman, T., Miller, L.D., Lee, K.C., Cartwright, C.A. Oncogene (2007) [Pubmed]
  7. Increased association of brain protein kinase C with the receptor for activated C kinase-1 (RACK1) in bipolar affective disorder. Wang, H., Friedman, E. Biol. Psychiatry (2001) [Pubmed]
  8. Protein kinase C signal transduction regulation in physiological and pathological aging. Battaini, F., Pascale, A. Ann. N. Y. Acad. Sci. (2005) [Pubmed]
  9. The nonword reading deficit in developmental dyslexia: evidence from children learning to read German. Wimmer, H. Journal of experimental child psychology. (1996) [Pubmed]
  10. RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Liu, Y.V., Baek, J.H., Zhang, H., Diez, R., Cole, R.N., Semenza, G.L. Mol. Cell (2007) [Pubmed]
  11. RACK1 mediates activation of JNK by protein kinase C [corrected]. López-Bergami, P., Habelhah, H., Bhoumik, A., Zhang, W., Wang, L.H., Ronai, Z. Mol. Cell (2005) [Pubmed]
  12. Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration. Osmanagic-Myers, S., Gregor, M., Walko, G., Burgstaller, G., Reipert, S., Wiche, G. J. Cell Biol. (2006) [Pubmed]
  13. Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy. Arya, R., Kedar, V., Hwang, J.R., McDonough, H., Li, H.H., Taylor, J., Patterson, C. J. Cell Biol. (2004) [Pubmed]
  14. Mutations in the cytoplasmic domain of P0 reveal a role for PKC-mediated phosphorylation in adhesion and myelination. Xu, W., Shy, M., Kamholz, J., Elferink, L., Xu, G., Lilien, J., Balsamo, J. J. Cell Biol. (2001) [Pubmed]
  15. Cloning, expression and genomic structure of a novel human GNB2L1 gene, which encodes a receptor of activated protein kinase C (RACK). Wang, S., Chen, J.Z., Zhang, Z., Gu, S., Ji, C., Tang, R., Ying, K., Xie, Y., Mao, Y. Mol. Biol. Rep. (2003) [Pubmed]
  16. The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway. Rigas, A.C., Ozanne, D.M., Neal, D.E., Robson, C.N. J. Biol. Chem. (2003) [Pubmed]
  17. Plectin-RACK1 (receptor for activated C kinase 1) scaffolding: a novel mechanism to regulate protein kinase C activity. Osmanagic-Myers, S., Wiche, G. J. Biol. Chem. (2004) [Pubmed]
  18. The N-terminus of the WD5 repeat of human RACK1 binds to airway epithelial NHERF1. Liedtke, C.M., Wang, X. Biochemistry (2006) [Pubmed]
  19. Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Ceci, M., Gaviraghi, C., Gorrini, C., Sala, L.A., Offenhäuser, N., Marchisio, P.C., Biffo, S. Nature (2003) [Pubmed]
  20. Interaction with factor associated with neutral sphingomyelinase activation, a WD motif-containing protein, identifies receptor for activated C-kinase 1 as a novel component of the signaling pathways of the p55 TNF receptor. Tcherkasowa, A.E., Adam-Klages, S., Kruse, M.L., Wiegmann, K., Mathieu, S., Kolanus, W., Krönke, M., Adam, D. J. Immunol. (2002) [Pubmed]
  21. Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex. Guillemot, F., Billault, A., Auffray, C. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  22. RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting protein, modulates IGF-I-dependent integrin signaling and promotes cell spreading and contact with extracellular matrix. Hermanto, U., Zong, C.S., Li, W., Wang, L.H. Mol. Cell. Biol. (2002) [Pubmed]
  23. 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. Chang, B.Y., Conroy, K.B., Machleder, E.M., Cartwright, C.A. Mol. Cell. Biol. (1998) [Pubmed]
  24. The anchoring protein RACK1 links protein kinase Cepsilon to integrin beta chains. Requirements for adhesion and motility. Besson, A., Wilson, T.L., Yong, V.W. J. Biol. Chem. (2002) [Pubmed]
  25. Photoinduced inactivation of protein kinase C by dequalinium identifies the RACK-1-binding domain as a recognition site. Rotenberg, S.A., Sun, X.G. J. Biol. Chem. (1998) [Pubmed]
  26. Tyrosine 302 in RACK1 is essential for insulin-like growth factor-I-mediated competitive binding of PP2A and beta1 integrin and for tumor cell proliferation and migration. Kiely, P.A., Baillie, G.S., Lynch, M.J., Houslay, M.D., O'Connor, R. J. Biol. Chem. (2008) [Pubmed]
  27. Tyrosine kinase 2 interacts with and phosphorylates receptor for activated C kinase-1, a WD motif-containing protein. Haro, T., Shimoda, K., Kakumitsu, H., Kamezaki, K., Numata, A., Ishikawa, F., Sekine, Y., Muromoto, R., Matsuda, T., Harada, M. J. Immunol. (2004) [Pubmed]
  28. RACK1 is an insulin-like growth factor 1 (IGF-1) receptor-interacting protein that can regulate IGF-1-mediated Akt activation and protection from cell death. Kiely, P.A., Sant, A., O'Connor, R. J. Biol. Chem. (2002) [Pubmed]
  29. Conformational analysis in solution of protein kinase C betaII V5-1 peptide. Shin, C., Ahn, J.H., Lim, Y. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  30. Identification of a surface on the beta-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5. Steele, M.R., McCahill, A., Thompson, D.S., MacKenzie, C., Isaacs, N.W., Houslay, M.D., Bolger, G.B. Cell. Signal. (2001) [Pubmed]
  31. Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction. Lee, H.S., Millward-Sadler, S.J., Wright, M.O., Nuki, G., Al-Jamal, R., Salter, D.M. Osteoarthr. Cartil. (2002) [Pubmed]
  32. RACK1 vs. HSP90: competition for HIF-1alpha degradation vs. stabilization. Liu, Y.V., Semenza, G.L. Cell Cycle (2007) [Pubmed]
  33. Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase. Kiely, P.A., Baillie, G.S., Barrett, R., Buckley, D.A., Adams, D.R., Houslay, M.D., O'Connor, R. J. Biol. Chem. (2009) [Pubmed]
  34. The WD motif-containing protein RACK-1 functions as a scaffold protein within the type I IFN receptor-signaling complex. Usacheva, A., Tian, X., Sandoval, R., Salvi, D., Levy, D., Colamonici, O.R. J. Immunol. (2003) [Pubmed]
  35. Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor. Croze, E., Usacheva, A., Asarnow, D., Minshall, R.D., Perez, H.D., Colamonici, O. J. Immunol. (2000) [Pubmed]
  36. 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. Usacheva, A., Smith, R., Minshall, R., Baida, G., Seng, S., Croze, E., Colamonici, O. J. Biol. Chem. (2001) [Pubmed]
 
WikiGenes - Universities