Biology:ACSL1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Long-chain-fatty-acid—CoA ligase 1 is an enzyme that in humans is encoded by the ACSL1 gene.[1][2][3]

Structure

Gene

The ACSL1 gene is located on the 4th chromosome, with its specific location being 4q35.1. The gene contains 28 exons.[3]

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.[3]

In melanocytic cells ACSL1 gene expression may be regulated by MITF.[4]

Function

The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation.[3] Several transcript variants encoding different isoforms have been found for this gene. This specific protein is most commonly found in mitochondria and peroxisomes.[5]

Clinical significance

ACSL1 is known to be involved in fatty-acid metabolism critical for heart function [6] and nonspecific mental retardation.[7] Since the ACSL4 gene is highly expressed in brain, where it encodes a brain specific isoform, an ASCL1 mutation may be an efficient diagnostic tool in mentally retarded males.[8]

Interactions

ACSL1 expression is regulated by SHP2 activity.[9] Additionally, ACSL4 interacts with ACSL3, APP, DSE, ELAVL1, HECW2, MINOS1, PARK2, SPG20, SUMO2, TP53, TUBGCP3, UBC, UBD, and YWHAQ.[3]

References

  1. ↑ "Structure and regulation of rat long-chain acyl-CoA synthetase". The Journal of Biological Chemistry 265 (15): 8681–5. May 1990. doi:10.1016/S0021-9258(19)38942-2. PMID 2341402. 
  2. ↑ "Chromosomal localization of the human gene for palmitoyl-CoA ligase (FACL1)". Cytogenetics and Cell Genetics 59 (1): 17–9. Feb 1992. doi:10.1159/000133189. PMID 1531127. 
  3. ↑ 3.0 3.1 3.2 3.3 3.4 "Entrez Gene: ACSL1 acyl-CoA synthetase long-chain family member 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2180. 
  4. ↑ "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell & Melanoma Research 21 (6): 665–76. Dec 2008. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. 
  5. ↑ "Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1170 (1): 44–52. Sep 1993. doi:10.1016/0005-2760(93)90174-8. PMID 8399326. 
  6. ↑ Lewandowski, Doug (2019), Scientists find metabolic target to prevent, treat heart failure at earliest stage (published March 2019), https://news.osu.edu/scientists-find-metabolic-target-to-prevent-treat-heart-failure-at-earliest-stage 
  7. ↑ "FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation". Nature Genetics 30 (4): 436–40. Apr 2002. doi:10.1038/ng857. PMID 11889465. 
  8. ↑ "A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients". Journal of Medical Genetics 40 (1): 11–7. Jan 2003. doi:10.1136/jmg.40.1.11. PMID 12525535. 
  9. ↑ "Tyrosine phosphatase SHP2 regulates the expression of acyl-CoA synthetase ACSL4". Journal of Lipid Research 52 (11): 1936–48. Nov 2011. doi:10.1194/jlr.m015552. PMID 21903867. 

Further reading

External links




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