Use at an assay dependent concentration. PubMed: 24312579
Non-catalytic component of the multisynthase complex. Stimulates the catalytic activity of cytoplasmic arginyl-tRNA synthase. Binds tRNA. Possesses inflammatory cytokine activity. Negatively regulates TGF-beta signaling through stabilization of SMURF2 by binding to SMURF2 and inhibiting its SMAD7-mediated degradation. Involved in glucose homeostasis through induction of glucagon secretion at low glucose levels. Promotes dermal fibroblast proliferation and wound repair. Regulates KDELR1-mediated retention of HSP90B1/gp96 in the endoplasmic reticulum. Plays a role in angiogenesis by inducing endothelial cell migration at low concentrations and endothelian cell apoptosis at high concentrations. Induces maturation of dendritic cells and monocyte cell adhesion. Modulates endothelial cell responses by degrading HIF-1A through interaction with PSMA7.
Involvement in disease
Defects in AIMP1 are the cause of leukodystrophy hypomyelinating type 3 (HLD3) [MIM:260600]. A severe autosomal recessive hypomyelinating leukodystrophy characterized by early infantile onset of global developmental delay, lack of development, lack of speech acquisition, and peripheral spasticity associated with decreased myelination in the central nervous system.
Contains 1 tRNA-binding domain.
Cleaved by caspase-7 in response to apoptosis to produce EMAP-II.
Nucleus. Cytoplasm > cytosol. Cytoplasmic vesicle > secretory vesicle. Secreted. Endoplasmic reticulum. Golgi apparatus. Enriched in secretory vesicles of pancreatic alpha cells and secreted from the pancreas in response to low glucose levels (By similarity). Also secreted in response to hypoxia and both apoptotic and necrotic cell death.
Park SJ et al. Evaluation of Multi-tRNA Synthetase Complex by Multiple Reaction Monitoring Mass Spectrometry Coupled with Size Exclusion Chromatography. PLoS One10:e0142253 (2015).
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Kim K et al. Reinvestigation of aminoacyl-TRNA synthetase core complex by affinity purification-mass spectrometry reveals TARSL2 as a potential member of the complex. PLoS One8:e81734 (2013).
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