α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase
α/β-hydrolase domain-containing 6 (ABHD6) belongs to the α/β-hydrolase fold superfamily and was originally discovered in a functional proteomic approach designed to discover monoacylglycerol (MAG) hydrolases in the mouse brain degrading the endocannabinoid 2-arachidonoylglycerol. Subsequent studies...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-08-01
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| Series: | Metabolites |
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| Online Access: | https://www.mdpi.com/2218-1989/12/8/761 |
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| author | Lisa-Maria Pusch Lina Riegler-Berket Monika Oberer Robert Zimmermann Ulrike Taschler |
| author_facet | Lisa-Maria Pusch Lina Riegler-Berket Monika Oberer Robert Zimmermann Ulrike Taschler |
| author_sort | Lisa-Maria Pusch |
| collection | DOAJ |
| description | α/β-hydrolase domain-containing 6 (ABHD6) belongs to the α/β-hydrolase fold superfamily and was originally discovered in a functional proteomic approach designed to discover monoacylglycerol (MAG) hydrolases in the mouse brain degrading the endocannabinoid 2-arachidonoylglycerol. Subsequent studies confirmed that ABHD6 acts as an MAG hydrolase regulating cannabinoid receptor-dependent and -independent signaling processes. The enzyme was identified as a negative modulator of insulin secretion and regulator of energy metabolism affecting the pathogenesis of obesity and metabolic syndrome. It has been implicated in the metabolism of the lysosomal co-factor bis(monoacylglycerol)phosphate and in the surface delivery of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors. Finally, ABHD6 was shown to affect cancer cell lipid metabolism and tumor malignancy. Here, we provide new insights into the experimentally derived crystal structure of ABHD6 and its possible orientation in biological membranes, and discuss ABHD6′s functions in health and disease. |
| first_indexed | 2024-03-09T04:05:24Z |
| format | Article |
| id | doaj.art-507818ac034641c687ce20efe75b990e |
| institution | Directory Open Access Journal |
| issn | 2218-1989 |
| language | English |
| last_indexed | 2024-03-09T04:05:24Z |
| publishDate | 2022-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Metabolites |
| spelling | doaj.art-507818ac034641c687ce20efe75b990e2023-12-03T14:06:27ZengMDPI AGMetabolites2218-19892022-08-0112876110.3390/metabo12080761α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid HydrolaseLisa-Maria Pusch0Lina Riegler-Berket1Monika Oberer2Robert Zimmermann3Ulrike Taschler4Institute of Molecular Biosciences, NAWI Graz, University of Graz, 8010 Graz, AustriaInstitute of Molecular Biosciences, NAWI Graz, University of Graz, 8010 Graz, AustriaInstitute of Molecular Biosciences, NAWI Graz, University of Graz, 8010 Graz, AustriaInstitute of Molecular Biosciences, NAWI Graz, University of Graz, 8010 Graz, AustriaInstitute of Molecular Biosciences, NAWI Graz, University of Graz, 8010 Graz, Austriaα/β-hydrolase domain-containing 6 (ABHD6) belongs to the α/β-hydrolase fold superfamily and was originally discovered in a functional proteomic approach designed to discover monoacylglycerol (MAG) hydrolases in the mouse brain degrading the endocannabinoid 2-arachidonoylglycerol. Subsequent studies confirmed that ABHD6 acts as an MAG hydrolase regulating cannabinoid receptor-dependent and -independent signaling processes. The enzyme was identified as a negative modulator of insulin secretion and regulator of energy metabolism affecting the pathogenesis of obesity and metabolic syndrome. It has been implicated in the metabolism of the lysosomal co-factor bis(monoacylglycerol)phosphate and in the surface delivery of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors. Finally, ABHD6 was shown to affect cancer cell lipid metabolism and tumor malignancy. Here, we provide new insights into the experimentally derived crystal structure of ABHD6 and its possible orientation in biological membranes, and discuss ABHD6′s functions in health and disease.https://www.mdpi.com/2218-1989/12/8/761ABHD6lipid hydrolasemonoacylglycerolbis(monoacylglycerol)phosphateinflammationmetabolic syndrome |
| spellingShingle | Lisa-Maria Pusch Lina Riegler-Berket Monika Oberer Robert Zimmermann Ulrike Taschler α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase Metabolites ABHD6 lipid hydrolase monoacylglycerol bis(monoacylglycerol)phosphate inflammation metabolic syndrome |
| title | α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase |
| title_full | α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase |
| title_fullStr | α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase |
| title_full_unstemmed | α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase |
| title_short | α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase |
| title_sort | α β hydrolase domain containing 6 abhd6 a multifunctional lipid hydrolase |
| topic | ABHD6 lipid hydrolase monoacylglycerol bis(monoacylglycerol)phosphate inflammation metabolic syndrome |
| url | https://www.mdpi.com/2218-1989/12/8/761 |
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