Receptor for activated C kinase 1

RACK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AOW, 4UG0, 4V6X, 5A2Q, 5AJ0, 5FLX
Identifiers
Aliases	RACK1, Gnb2-rs1, H12.3, HLC-7, PIG21, GNB2L1, receptor for activated C kinase 1
External IDs	OMIM: 176981; MGI: 101849; HomoloGene: 4446; GeneCards: RACK1; OMA:RACK1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q35.3 Start 181,236,897 bp End 181,248,096 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 B1.2 Start 48,691,159 bp End 48,697,261 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pericardium superior surface of tongue body of tongue mucosa of pharynx vena cava nipple saphenous vein trachea lower lobe of lung cerebellar vermis Top expressed in epiblast ventricular zone bone marrow ovary ganglionic eminence spleen uterus zone of skin placenta morula More reference expression data BioGPS n/a
Gene ontology Molecular function protein homodimerization activity receptor tyrosine kinase binding SH2 domain binding signaling adaptor activity protein tyrosine kinase inhibitor activity protein binding enzyme binding cysteine-type endopeptidase activator activity involved in apoptotic process molecular adaptor activity protein phosphatase binding signaling receptor binding ion channel inhibitor activity RNA binding cadherin binding ribosome binding protein kinase C binding cyclin binding Cellular component cytoplasm cell body perikaryon cell projection membrane plasma membrane soma dendrite midbody mitochondrion perinuclear region of cytoplasm neuron projection phagocytic cup extracellular exosome nucleus IRE1-RACK1-PP2A complex nucleoplasm cytosol ribosome small ribosomal subunit cytosolic small ribosomal subunit Biological process positive regulation of protein homooligomerization positive regulation of Golgi to plasma membrane protein transport negative regulation of protein kinase B signaling positive regulation of protein phosphorylation positive regulation of ceramide biosynthetic process regulation of cell division negative regulation of phagocytosis positive regulation of gastrulation rhythmic process positive regulation of cell migration negative regulation of endoplasmic reticulum unfolded protein response cellular response to growth factor stimulus negative regulation of Wnt signaling pathway regulation of tumor necrosis factor-mediated signaling pathway negative regulation of gene expression regulation of cell cycle regulation of protein localization multicellular organism development positive regulation of GTPase activity negative regulation of hydrogen peroxide-induced neuron death positive regulation of mitochondrial depolarization gastrulation negative regulation of cell growth negative regulation of peptidyl-serine phosphorylation positive regulation of apoptotic process cell cycle regulation of growth viral process regulation of establishment of cell polarity activation of cysteine-type endopeptidase activity involved in apoptotic process positive regulation of intrinsic apoptotic signaling pathway regulation of translation positive regulation of proteasomal ubiquitin-dependent protein catabolic process cellular response to glucose stimulus positive regulation of cyclic-nucleotide phosphodiesterase activity apoptotic process negative regulation of protein tyrosine kinase activity protein biosynthesis pigmentation protein ubiquitination rescue of stalled ribosome negative regulation of translation regulation of protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10399 14694 Ensembl ENSG00000204628 ENSMUSG00000020372 UniProt P63244 P68040 RefSeq (mRNA) NM_006098 NM_008143 RefSeq (protein) NP_006089 NP_032169 Location (UCSC) Chr 5: 181.24 – 181.25 Mb Chr 11: 48.69 – 48.7 Mb PubMed search
Wikidata
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Receptor for activated C kinase 1 (RACK1), also known as guanine nucleotide-binding protein subunit beta-2-like 1 (GNB2L1), is a 35 kDa protein that in humans is encoded by the RACK1 gene.

Function

RACK1 was originally isolated and identified as an intracellular protein receptor for protein kinase C, noting the significant homology to the beta subunit of heterotrimeric G proteins. Later studies established RACK1, and its yeast homolog Asc1, as a core ribosomal protein of the eukaryotic small (40S) ribosomal subunit. Much of the function of Asc1/RACK1 appears to result from its position on the 'head' of the 40S ribosomal subunit. Asc1/RACK1 participates in several aspects of eukaryotic translation and ribosome quality control, including IRES-mediated translation, non-stop decay, non-functional 18S ribosomal RNA decay, and frameshifting.

Interactions

RACK1 is positioned at the solvent-exposed surface of the 40S ribosomal subunit, where it is held in place through contacts with both the 18S rRNA and other ribosomal proteins, including uS3, uS9, and eS17. Additionally, RACK1 has been shown to interact with:

• AGTRAP
• Androgen receptor,
• CD18,
• CD29
• Cyclin A1
• EIF6,
• FYN,
• IFNAR2,
• Janus kinase 1
• OTUB1,
• P73,
• PDE4D,
• PRKCB1,
• PRKCE,
• PTPRM,
• RAS p21 protein activator 1,
• ST7,
• STAT1,
• Src, and
• Tyrosine kinase 2.

See also

• Eukaryotic small ribosomal subunit (40S)
• Protein kinase C
• Heterotrimeric G protein

Further reading

• Liu YV, Semenza GL (March 2007). "RACK1 vs. HSP90: competition for HIF-1 alpha degradation vs. stabilization". Cell Cycle. 6 (6): 656–9. doi:10.4161/cc.6.6.3981. PMID 17361105.
• Mochly-Rosen D, Miller KG, Scheller RH, Khaner H, Lopez J, Smith BL (September 1992). "p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C". Biochemistry. 31 (35): 8120–4. doi:10.1021/bi00150a003. PMID 1326322.
• Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Pumiglia KM, LeVine H, Haske T, Habib T, Jove R, Decker SJ (June 1995). "A direct interaction between G-protein beta gamma subunits and the Raf-1 protein kinase". The Journal of Biological Chemistry. 270 (24): 14251–4. doi:10.1074/jbc.270.24.14251. PMID 7782277.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Disatnik MH, Hernandez-Sotomayor SM, Jones G, Carpenter G, Mochly-Rosen D (January 1994). "Phospholipase C-gamma 1 binding to intracellular receptors for activated protein kinase C". Proceedings of the National Academy of Sciences of the United States of America. 91 (2): 559–63. Bibcode:1994PNAS...91..559D. doi:10.1073/pnas.91.2.559. PMC 42988. PMID 8290562.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Liliental J, Chang DD (January 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". The Journal of Biological Chemistry. 273 (4): 2379–83. doi:10.1074/jbc.273.4.2379. PMID 9442085.
• Chang BY, Conroy KB, Machleder EM, Cartwright CA (June 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. doi:10.1128/mcb.18.6.3245. PMC 108906. PMID 9584165.
• Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (October 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". The Journal of Biological Chemistry. 273 (42): 27459–66. doi:10.1074/jbc.273.42.27459. PMID 9765275.
• Shimohama S, Kamiya S, Taniguchi T, Kimura J (December 1998). "Intracellular receptors for activated C-kinase in the postmortem human brain: no alteration in Alzheimer disease". Alzheimer Disease and Associated Disorders. 12 (4): 384–6. doi:10.1097/00002093-199812000-00022. PMID 9876970.
• 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. doi:10.1074/jbc.274.21.14909. PMID 10329691.
• Ron D, Jiang Z, Yao L, Vagts A, Diamond I, Gordon A (September 1999). "Coordinated movement of RACK1 with activated betaIIPKC". The Journal of Biological Chemistry. 274 (38): 27039–46. doi:10.1074/jbc.274.38.27039. PMID 10480917.
• Geijsen N, Spaargaren M, Raaijmakers JA, Lammers JW, Koenderman L, Coffer PJ (September 1999). "Association of RACK1 and PKCbeta with the common beta-chain of the IL-5/IL-3/GM-CSF receptor". Oncogene. 18 (36): 5126–30. doi:10.1038/sj.onc.1202896. PMID 10490850.
• Smith PR, de Jesus O, Turner D, Hollyoake M, Karstegl CE, Griffin BE, Karran L, Wang Y, Hayward SD, Farrell PJ (April 2000). "Structure and coding content of CST (BART) family RNAs of Epstein-Barr virus". Journal of Virology. 74 (7): 3082–92. doi:10.1128/JVI.74.7.3082-3092.2000. PMC 111807. PMID 10708423.
• Ellis JH, Ashman C, Burden MN, Kilpatrick KE, Morse MA, Hamblin PA (June 2000). "GRID: a novel Grb-2-related adapter protein that interacts with the activated T cell costimulatory receptor CD28". Journal of Immunology. 164 (11): 5805–14. doi:10.4049/jimmunol.164.11.5805. PMID 10820259.
• Croze E, Usacheva A, Asarnow D, Minshall RD, Perez HD, Colamonici O (November 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. doi:10.4049/jimmunol.165.9.5127. PMID 11046044.
• Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.