scholarly journals CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase

2009 ◽  
Vol 51 (4) ◽  
pp. 709-719 ◽  
Author(s):  
Gabriela Montero-Moran ◽  
Jorge M. Caviglia ◽  
Derek McMahon ◽  
Alexis Rothenberg ◽  
Vidya Subramanian ◽  
...  
Keyword(s):  
Lysophosphatidic Acid ◽  
Coenzyme A ◽  
Lysophosphatidic Acid Acyltransferase

scholarly journals At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase

2009 ◽  
Vol 151 (2) ◽  
pp. 869-881 ◽  
Author(s):  
Ananda K. Ghosh ◽  
Neha Chauhan ◽  
Sona Rajakumari ◽  
Guenther Daum ◽  
Ram Rajasekharan
Keyword(s):  
Lysophosphatidic Acid ◽  
Coenzyme A ◽  
Lysophosphatidic Acid Acyltransferase ◽  
Acyl Coenzyme A

scholarly journals Lysophosphatidic Acid Acyltransferase β (LPAATβ) Promotes the Tumor Growth of Human Osteosarcoma

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e14182 ◽  
Author(s):  
Farbod Rastegar ◽  
Jian-Li Gao ◽  
Deana Shenaq ◽  
Qing Luo ◽  
Qiong Shi ◽  
...  
Keyword(s):  
Tumor Growth ◽  
Lysophosphatidic Acid ◽  
Human Osteosarcoma ◽  
Lysophosphatidic Acid Acyltransferase

scholarly journals Human Lysophosphatidic Acid Acyltransferase

1997 ◽  
Vol 272 (32) ◽  
pp. 20299-20305 ◽  
Author(s):  
Christine Eberhardt ◽  
Patrick W. Gray ◽  
Larry W. Tjoelker
Keyword(s):  
Lysophosphatidic Acid ◽  
Lysophosphatidic Acid Acyltransferase

scholarly journals YPR139c/LOA1encodes a novel lysophosphatidic acid acyltransferase associated with lipid droplets and involved in TAG homeostasis

2012 ◽  
Vol 23 (2) ◽  
pp. 233-246 ◽  
Author(s):  
Sophie Ayciriex ◽  
Marina Le Guédard ◽  
Nadine Camougrand ◽  
Gisèle Velours ◽  
Mario Schoene ◽  
...  
Keyword(s):  
Lysophosphatidic Acid ◽  
Lipid Droplets ◽  
Neutral Lipids ◽  
In Vitro Assays ◽  
Metabolic Labeling ◽  
Lysophosphatidic Acid Acyltransferase ◽  
Escherichia Coli Cells ◽  
Type Strains

For many years, lipid droplets (LDs) were considered to be an inert store of lipids. However, recent data showed that LDs are dynamic organelles playing an important role in storage and mobilization of neutral lipids. In this paper, we report the characterization of LOA1 (alias VPS66, alias YPR139c), a yeast member of the glycerolipid acyltransferase family. LOA1 mutants show abnormalities in LD morphology. As previously reported, cells lacking LOA1 contain more LDs. Conversely, we showed that overexpression results in fewer LDs. We then compared the lipidome of loa1Δ mutant and wild-type strains. Steady-state metabolic labeling of loa1Δ revealed a significant reduction in triacylglycerol content, while phospholipid (PL) composition remained unchanged. Interestingly, lipidomic analysis indicates that both PLs and glycerolipids are qualitatively affected by the mutation, suggesting that Loa1p is a lysophosphatidic acid acyltransferase (LPA AT) with a preference for oleoyl-CoA. This hypothesis was tested by in vitro assays using both membranes of Escherichia coli cells expressing LOA1 and purified proteins as enzyme sources. Our results from purification of subcellular compartments and proteomic studies show that Loa1p is associated with LD and active in this compartment. Loa1p is therefore a novel LPA AT and plays a role in LD formation.

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