| Title : Human alpha beta hydrolase domain containing protein 11 and its yeast homolog are lipid hydrolases - Arya_2017_Biochem.Biophys.Res.Commun_487_875 |
| Author(s) : Arya M , Srinivasan M , Rajasekharan R |
| Ref : Biochemical & Biophysical Research Communications , 487 :875 , 2017 |
| Abstract : Mammalian alpha/beta hydrolase domain (ABHD) family of proteins have emerged as key regulators of lipid metabolism and are found to be associated with human diseases. Human alpha/beta-hydrolase domain containing protein 11 (ABHD11) has recently been predicted as a potential biomarker for human lung adenocarcinoma. In silico analyses of the ABHD11 protein sequence revealed the presence of a conserved lipase motif GXSXG. However, the role of ABHD11 in lipid metabolism is not known. To understand the biological function of ABHD11, we heterologously expressed the human ABHD11 in budding yeast, Saccharomyces cerevisiae. In vivo [14C]acetate labeling of cellular lipids in yeast cells overexpressing ABHD11 showed a decrease in triacylglycerol content. Overexpression of ABHD11 also alters the molecular species of triacylglycerol in yeast. Similar activity was observed in its yeast homolog, Ygr031w. The role of the conserved lipase motif in the hydrolase activity was proven by the mutation of all conserved amino acid residues of GXSXG motif. Collectively, our results demonstrate that human ABHD11 and its yeast homolog YGR031W have a pivotal role in the lipid metabolism. |
| ESTHER : Arya_2017_Biochem.Biophys.Res.Commun_487_875 |
| PubMedSearch : Arya_2017_Biochem.Biophys.Res.Commun_487_875 |
| PubMedID: 28465236 |
| Gene_locus related to this paper: human-ABHD11 |
| Gene_locus related to this paper: human-ABHD11 |
Arya M, Srinivasan M, Rajasekharan R (2017)
Human alpha beta hydrolase domain containing protein 11 and its yeast homolog are lipid hydrolases
Biochemical & Biophysical Research Communications
487 :875
Arya M, Srinivasan M, Rajasekharan R (2017)
Biochemical & Biophysical Research Communications
487 :875