Recombinant Mouse Acetyl-coenzyme A synthetase, cytoplasmic (Acss2)

Function

Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:11150295, PubMed:16790548, PubMed:28562591). Acetate is the preferred substrate but can also utilize propionate with a much lower affinity (PubMed:11150295). Catalyzes the conversion of lactate into lactoyl-CoA (By similarity). Does not catalyze the conversion of butyrate or crotonate to their corresponding acyl-CoAs (By similarity). Nuclear ACSS2 promotes glucose deprivation-induced lysosomal biogenesis and autophagy, tumor cell survival and brain tumorigenesis (By similarity). Glucose deprivation results in AMPK-mediated phosphorylation of ACSS2 leading to its translocation to the nucleus where it binds to TFEB and locally produces acetyl-CoA for histone acetylation in the promoter regions of TFEB target genes thereby activating their transcription (By similarity). The regulation of genes associated with autophagy and lysosomal activity through ACSS2 is important for brain tumorigenesis and tumor survival (By similarity). Acts as a chromatin-bound transcriptional coactivator that up-regulates histone acetylation and expression of neuronal genes (PubMed:28562591). Can be recruited to the loci of memory-related neuronal genes to maintain a local acetyl-CoA pool, providing the substrate for histone acetylation and promoting the expression of specific genes, which is essential for maintaining long-term spatial memory (PubMed:28562591)

Subcellular Location

Cytoplasm, cytosol; Cytoplasm; Nucleus

Tissue Specificity

Expressed in the hippocampus

Subunit

Monomer (By similarity). Interacts with TFEB (By similarity). AMPK-mediated phosphorylated form at Ser-659 interacts with KPNA1; this interaction results in nuclear translocation of ACSS2 (By similarity). Interacts with the 'Thr-172' phosphorylated form of PRKAA2 (By similarity). Interacts with CREBBP (PubMed:28562591)

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• Fujino T. et al. Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. — J. Biol. Chem. (2001)
• Hallows W.C. et al. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. — Proc. Natl. Acad. Sci. U.S.A. (2006)
• Munton R.P. et al. Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations. — Mol. Cell. Proteomics (2007)
• Villen J. et al. Large-scale phosphorylation analysis of mouse liver. — Proc. Natl. Acad. Sci. U.S.A. (2007)