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Acyl-CoA synthetase long-chain family member 3

ACSL3, ACS3, FACL3, acyl-CoA synthetase long-chain family member 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. This isozyme is highly expressed in brain, and preferentially utilizes myristate, arachidonate, and eicosapentaenoate as substrates. The amino acid sequence of this isozyme is 92% identical to that of rat homolog. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on ACSL3
The N-terminal region of acyl-CoA synthetase 3 is essential for both the localization on lipid droplets and the function in fatty acid uptake.
F├╝llekrug et al., Heidelberg, Germany. In J Lipid Res, 2012
role of N-terminal region of acyl-CoA synthetase 3 in its function and localization on lipid droplets
ACSL3 and GSK-3╬▓ are essential for lipid upregulation induced by endoplasmic reticulum stress in liver cells.
Lai et al., Tainan City, Taiwan. In J Cell Biochem, 2011
expression of ACSL3 was induced by endoplasmic reticulum stress
The Lyn kinase C-lobe mediates Golgi export of Lyn through conformation-dependent ACSL3 association.
Yamaguchi et al., Chiba, Japan. In J Cell Sci, 2010
Results suggest that initiation of Golgi export of Lyn involves association of ACSL3 with the Lyn C-lobe, which is exposed to the molecular surface in an open conformation.
Activation of LXR increases acyl-CoA synthetase activity through direct regulation of ACSL3 in human placental trophoblast cells.
Nebb et al., Oslo, Norway. In J Lipid Res, 2010
Results suggest that liver X receptors play a regulatory role in fatty acid metabolism by direct regulation of ACSL3 in human placental trophoblast cells.
Long chain acyl-CoA synthetase-3 is a molecular target for peroxisome proliferator-activated receptor delta in HepG2 hepatoma cells.
Liu et al., Palo Alto, United States. In J Biol Chem, 2010
ACSL3 is a novel molecular target of PPARdelta in HepG2 cells; there is a regulatory mechanism for ACSL3 transcription in liver tissue
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