Recombinant Human Lysine--tRNA ligase (KARS)

1. The studies showed that mutations in KARS lead to a newly defined subtype of leukoencephalopathy associated with sensorineural hearing impairment. The combined effect of reduced aminoacylation and release of LysRS from the multiple-synthetase complex (MSC) likely underlies the pathogenesis of the KARS mutations identified in this study. PMID: 28887846
2. Using the TruSight One sequencing panel we identified two novel mutations in KARS. Both mutations, never reported previously, occur in a highly conserved region of the catalytic domain and displayed a dramatic effect on KARS stability PMID: 27891585
3. Caspase-8 controls the secretion of inflammatory lysyl-tRNA synthetase in exosomes from colorectal cancer cells. PMID: 28611052
4. Results indicate that KRS can promote cell-cell and cellextracellular matrix adhesion for migration. PMID: 26891990
5. finding show that enzymatically active Shiga toxins trigger the dissociation of lysyl-tRNA synthetase (KRS) from the multi-aminoacyl-tRNA synthetase complex in human macrophage-like differentiated THP-1 cells and its subsequent secretion. PMID: 26643967
6. KRS at the plasma membrane plays new roles in metastatic migration as a signaling inducer, and causes intracellular signaling for cancer dissemination PMID: 26091349
7. tRK1 forms a complex with human enolases and interacts with tRK1 and human pre-lysyl-tRNA synthetase (preKARS2) PMID: 25918939
8. structural characteristics of the KRS-LR interaction on the cell surface PMID: 24983501
9. Lysyl-tRNA synthetase plays essential role in HIV replication, transcriptional regulation, cytokine-like signaling. [review] PMID: 23972532
10. The role of preKARS2 in the tRNA mitochondrial import. PMID: 23799079
11. The KARS variant is identified in two families affected by DFNB89-associated autosomal-recessive nonsyndromic hearing impairment. PMID: 23768514
12. C-terminal domain of HIV-1 capsid protein as surrogate for human lysyl tRNA synthetase PMID: 23208549
13. A single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription. PMID: 23159739
14. Dual role for motif 1 residues of human lysyl-tRNA synthetase in dimerization and packaging into HIV-1. PMID: 23095741
15. The work thus unveiled a unique function of KRS in the control of cell migration and its pathological implication in metastasis. PMID: 22751010
16. Data are consistent with hypothesis that maturation of cytoplasmic KARS precursor is needed to reveal the potent tRNA binding properties of mitochondrial KARS. PMID: 22235746
17. LysRS associates with the Pol domain of GagPol. PMID: 21763493
18. The results suggest that this unique geometry, which reconfigures the LysRS tetramer from alpha(2):alpha(2) to alpha(2)beta(1):beta(1)alpha(2), is designed to control both retention and mobilization of LysRS from the multi-tRNA synthetase complex PMID: 21536907
19. The interaction between helix 7 of LysRS and helix 4 of the capsid C-terminal domain of HIV-1 Gag (HIV-CA-CTD) was studied using circular dichromism spectroscopy and molecular dynamics simulation. PMID: 21093454
20. These results underscore the contribution of KARS to the emission of (one of) the principal signal(s) of immunogenic cell death, CRT exposure. PMID: 20699648
21. Loss-of-function lysyl-tRNA synthetase mutations associated with peripheral neuropathy and Charcot-Marie-Tooth disease. PMID: 20920668
22. HIV-1 Gag interacts with human lysyl-tRNA synthetase during viral assembly PMID: 12756246
23. packaged into human immunodeficiency virus type 1 (HIV-1) via its interaction with Gag; this enzyme facilitates the selective packaging of tRNA(3)(Lys), the primer for initiating reverse transcription, into HIV-1 PMID: 15220430
24. analysis of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase PMID: 16702215
25. HIV-1 Vpr fulfills an essential role in the process of packaging of mitochondrial Lysyl-tRNA synthase. PMID: 17560997
26. This work reports further characterization of the interaction between HIV-1 capsid domain of Gag and human LysRS using truncation constructs and point mutations in the putative interaction helices. PMID: 17724017
27. present a 2.3-A crystal structure of a tetrameric form of human LysRS PMID: 18272479
28. mitoKARS is the first described member of a group of mitochondrial proteins whose interaction with mutant SOD1 contributes to mitochondrial dysfunction in ALS PMID: 18715867

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HGNC: 6215

OMIM: 601421

KEGG: hsa:3735

STRING: 9606.ENSP00000325448

UniGene: Hs.3100