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RACK1-GNB2L1 Protein, Antibody, ELISA Kit, cDNA Clone

RACK1-GNB2L1 Related Areas

RACK1-GNB2L1 Related Pathways

RACK1-GNB2L1 Related Product

    RACK1-GNB2L1 Summary & Protein Information

    RACK1-GNB2L1 Background

    Subunit structure: Component of the small (40S) ribosomal subunit (By similarity). Interacts with the 80S ribosome. Exists as a monomer and also forms oligomers. Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of GNB2L1/RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with LARP4B. Interacts with Y.pseudotuberculosis yopK. Interacts with a number of viral proteins including Epstein-Barr virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef phosphorylation by PKC.
    Subcellular location: Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Nucleus. Perikaryon (By similarity). Cell projection, dendrite (By similarity). Cell projection, phagocytic cup. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery. In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei. Localized to phagocytic cups following infection by Y.pestis.
    Tissue specificity: In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue.
    Post-translational: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.
    Sequence similarity: Belongs to the WD repeat G protein beta family.
    Contains 7 WD repeats.
    General information above from UniProt

    RACK1 (guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1), also known as GNB2L1, contains 7 WD repeats and belongs to the WD repeat G protein beta family. In the liver, RACK1 is expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. It is up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue. RACK1 is involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. It interacts with a wide variety of proteins and plays a role in many cellular processes. GNB2L1 binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. RACK1 may recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. It inhibits the activity of SRC kinases including SRC, LCK and YES1. RACK1 also inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. It enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer.

    RACK1-GNB2L1 Alternative Name

    RACK1-GNB2L1 Related Studies

  • Jannot G, et al.. (2011) The ribosomal protein RACK1 is required for microRNA function in both C. elegans and humans. EMBO Rep. 12(6):581-6.
  • Wang F, et al. (2011) RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3K/Akt pathway. J Biol Chem. 286(11):9097-106.
  • Cao XX, et al. (2011) RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway. Breast Cancer Res Treat. 126(3):555-63.
  • Myklebust LM, et al. (2011) Receptor for activated protein C kinase 1 (RACK1) is overexpressed in papillary thyroid carcinoma. Thyroid. 21(11):1217-25.
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