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sensitive to freezing3(sfr3) is a missense mutation in aminoglycoside N1-acetyltransferase. Freezing sensitivity of sfr3 appears to be due to cuticular deficiencies that develop during cold acclimation.
The gsd1 locus was mapped to chromosome 1, and the causal gene was identified as a new allele of Acetyl-Coenzyme A Carboxylase1 (ACC1), a gene encoding the main enzyme in cytosolic malonyl-coenzyme A synthesis.
Data suggest that the lack of cytosolic malonyl-CoA is likely to be the initial factor leading to abnormal development in acetyl-CoA carboxylase 1 mutants.
These results support the idea that C-rich sequences within the promoters (PI and PII) of ACC1 can form intramolecular i-motif structures, cause suppression of transcription, and thus reveal the functional significance of C-rich sequences in the regulation of ACC1 gene expression.
Among the proteins differentially expressed after treatment with exosome-like nanoparticles from Citrus-limon juice, we found a significant downregulation of the Acetyl-CoA Carboxylase 1 (ACACA) and we demonstrated that silencing ACACA in cancer cells leads to a reduction of cell growth.
Results show that the phosphorylation of the N-terminal regulatory domain decreases ACC1 activity, while phosphorylation in its central domain has no effect. Inhibition of the activity by phosphorylation is significantly more profound at citrate concentrations below 2 mm. Furthermore, deletion of the N-terminal domain facilitates structural changes induced by citrate, including conversion of ACC dimers to linear polymers.
cryo-electron microscopy structures of an ACC1 activated filament that is allosterically induced by citrate (ACC-citrate), and an inactivated filament form that results from binding of the BRCT domains of the breast cancer type 1 susceptibility protein (BRCA1)
These data showed that ACC1 gene (ACACA) expression was twofold greater in HCC compared to non-cancerous liver.
the present studies report for the first time a role of ACC1 in suppressing breast cancer migration and invasion by an fatty acid synthesis-independent, but acetyl-CoA-dependent, impact on the epithelial-mesenchymal transition programs in breast tumor cells and its subsequent importance for tumor invasion and recurrence.
the presence of an internal ribosome entry site in the ACC1 5' UTR allows ACC1 mRNA translation in conditions that are inhibitory to cap-dependent translation.
of ACCs decreased polyunsaturated fatty acid (PUFA) concentrations in liver due to reduced malonyl-CoA, which is required for elongation of essential fatty acids.
Inhibition of Acetyl-CoA Carboxylase 1 (ACC1) and 2 (ACC2) Reduces Proliferation and De Novo Lipogenesis of EGFRvIII Human Glioblastoma Cells
Cetuximab-mediated activation of AMPK and subsequent phosphorylation and inhibition of ACC is followed by a compensatory increase in total ACC, which rewires cancer metabolism from glycolysis-dependent to lipogenesis-dependent.
acetyl-CoA carboxylase 1 and senescence regulation in human fibroblasts involves oxidant mediated p38 MAPK activation
ACC1 and ACLY regulate the levels of ETV4 under hypoxia via increased alpha-ketoglutarate. These results reveal that the ACC1/ACLY-alpha-ketoglutarate-ETV4 axis is a novel means by which metabolic states regulate transcriptional output
Phospho-acetyl-CoA carboxylase protein expression correlates with tumor grade and the disease stage in gastric cancer.
ACAT1, ACACA, ALDH6A1 and MTHFD1 represent novel biomarkers in adipose tissue associated with type 2 diabetes in obese individuals.
ACACA may constitute a previously unrecognized target for novel anti-breast cancer stem cell therapies.
Single nucleotide polymorphisms in the ACACA and ACLY genes are associated with a relative change in plasma triglycierides following fish oil supplementation.
Exercise training increased AMPKalpha1 activity in older men, however, AMPKalpha2 activity, and the phosphorylation of AMPK, ACC and mTOR, were not affected
Metabolic regulation of invadopodia and invasion by acetyl-CoA carboxylase 1 and de novo lipogenesis.
IGF-1 reduced ACCalpha phosphorylation via an ATM/AMPK signaling pathway and suppressed ACCalpha expression through an ERK1/2
three major enzymes of the pathway, FASN, ACC, and ACLY, are up-regulated in numerous tumor types.
Polymorphisms of the ACACA and SREBF1 genes are promising markers for pig carcass and performance traits.
Alternative splicing of exon 28, which has been consistently described in human, rat and sheep has now been found in pigs.
Expression profiles showed that PI is the promoter driving expression of the dominant ACACA-transcript in brain.
Since the promoter region, PIII, is specific to mammary gland during lactation, the altered expression of the ACACA gene owing to the SNPs in the PIII region may influence the fatty acid composition in the milk.
results suggested that the SNPs in the promoter I region of ACACA gene are associated with variations in the fatty acid contents in longissimus dorsi muscle.
Using mice with Ser(79)Ala/Ser(212)Ala knock-in mutations (ACC DKI) the authors find that inhibition of ACC phosphorylation leads to reduced appetite in response to fasting or cold exposure.
AMPK-ACC signaling is coupled to the control of thrombosis by specifically modulating thromboxane and granule release in response to collagen.
Lipogenesis is dispensable for liver tumorigenesis in mice treated with diethylnitrosamine, and ACC enzymes have an important role in redox regulation and cell survival.
madecassic acid was the active form of madecassoside in ameliorating colitis by restoring the Th17/Treg balance via regulating the PPARgamma/AMPK/ACC1 pathway.
Studied a role for ACAC inactivation in meiotic resumption by testing the effect of two ACAC inhibitors, CP-640186 and Soraphen A, on mouse oocytes maintained in meiotic arrest in vitro.
AMPK-dependent inactivation of ACC is not essential for the control of myocardial FAO and subsequent cardiac function during a variety of conditions involving AMPK-independent and AMPK-dependent metabolic adaptations.
Results suggest an essential role for acetyl coenzyme A carboxylase 1 (ACC1)-mediated de novo lipogenesis as a regulator of CD8(+) T cell expansion.
the stimulation of fatty acid oxidation by modulating the AMPK-ACC-CPT-1 pathway may be part of a protective mechanism against saturated free fatty acids that drive podocyte death.
our data suggest that renin synthesis and secretion are regulated by AMPK and coupled to metabolism by phosphorylation of ACC1.
analysis of mRNA abundance and expression of SLC27A, ACC, SCD, FADS, LPIN, INSIG, and PPARGC1 gene isoforms in mouse mammary glands during the lactation cycle
A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis
Expression of the isoenzyme of Acc1 is mediated by MyoD and MRF4 is differentially affected by retinoic acid receptor and retinoid X receptor.
Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal.
when fed fat-free diet for 10 days, there was significant up-regulation of PPARgamma and several enzymes in the lipogenic pathway in the liver of liver-specific ACC1 knockout mice compared with the WT mice
description of a pathway in which Tribbles 3 (TRB3) stimulates lipolysis by triggering the degradation of acetyl-coenzyme A carboxylase (ACC) in adipose tissue; TRB3 promoted ACC ubiquitination through an association with the E3 ubiquitin ligase COP1
Hepatic de novo lipogenesis is present in liver-specific ACC1-deficient mice.
Downregulation of ACC1 on osteoblastogenesis may be the cause for the osteopenia phenotype of FACC1 knockout bone homeostasis.
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene.
acetyl-Coenzyme A carboxylase alpha
, acetyl-CoA carboxylase 1
, acetyl-coenzyme A carboxylase alpha
, acetyl-CoA carboxylase-alpha
, acetyl-CoA carboxylase
, acetyl coenzyme A carboxylase alpha
, acetyl-CoA carboxylase 265