KARS (gene)

KARS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases KARS, CMTRIB, DFNB89, KARS1, KARS2, KRS, Lysyl-tRNA synthetase
External IDs MGI: 1934754 HomoloGene: 4053 GeneCards: KARS
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

3735

85305

Ensembl

ENSG00000065427

ENSMUSG00000031948

UniProt

Q15046

Q99MN1

RefSeq (mRNA)

NM_005548
NM_001130089

NM_001130868
NM_001286384
NM_053092

RefSeq (protein)

NP_001123561.1
NP_005539.1

NP_444322.1

Location (UCSC) Chr 16: 75.63 – 75.65 Mb Chr 8: 111.99 – 112.01 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Lysyl-tRNA synthetase is an enzyme that in humans is encoded by the KARS gene.[3][4][5]

Function

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis[5]

Besides its role in translation, Lysyl-tRNA synthetase is involved in a signaling pathway leading to gene activation.[6] Following physiological stimulation of a variety of cells, Lysyl-tRNA synthetase binds to the transcription factors MITF[7] and USF2[8] and can then influence their transcriptional activities. Such physiological stimulation includes immunological activation of mast cells, so this pathway maybe relevant to the allergic response.

Interactions

KARS (gene) has been shown to interact with Multisynthetase complex auxiliary component p38.[9][10] Physiological trigger such as immunological activation results in the phosphorylation of LysRS is on serine residues. It separates from the multisynthetase complex and initiates Ap4A production.[6]

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. Nichols RC, Blinder J, Pai SI, Ge Q, Targoff IN, Plotz PH, Liu P (Aug 1996). "Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24". Genomics. 36 (1): 210–3. doi:10.1006/geno.1996.0449. PMID 8812440.
  4. Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P (Sep 1997). "Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant". The Journal of Biological Chemistry. 272 (36): 22809–16. doi:10.1074/jbc.272.36.22809. PMID 9278442.
  5. 1 2 "Entrez Gene: KARS lysyl-tRNA synthetase".
  6. 1 2 Yannay-Cohen N, Carmi-Levy I, Kay G, Yang CM, Han JM, Kemeny DM, Kim S, Nechushtan H, Razin E (Jun 2009). "LysRS serves as a key signaling molecule in the immune response by regulating gene expression". Molecular Cell. 34 (5): 603–11. doi:10.1016/j.molcel.2009.05.019. PMID 19524539.
  7. Lee YN, Nechushtan H, Figov N, Razin E (Feb 2004). "The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells". Immunity. 20 (2): 145–51. doi:10.1016/S1074-7613(04)00020-2. PMID 14975237.
  8. Lee YN, Razin E (Oct 2005). "Nonconventional involvement of LysRS in the molecular mechanism of USF2 transcriptional activity in FcepsilonRI-activated mast cells". Molecular and Cellular Biology. 25 (20): 8904–12. doi:10.1128/MCB.25.20.8904-8912.2005. PMC 1265770Freely accessible. PMID 16199869.
  9. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  10. Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (Jan 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.

Further reading

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