Molecular and biochemical characterizations of the monoacylglycerol lipase gene family of <i>Arabidopsis thaliana</i>

Kim, Ryeo Jin; Kim, Hae Jin; Shim, Donghwan; Suh, Mi Chung

doi:10.1111/tpj.13146

Cited by 56 publications

(63 citation statements)

References 67 publications

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“…Then, the new ester between the serine and the FA is hydrolyzed. Examples for characterized GXSXG-lipases in Arabidopsis are the MAG and 1,3-DAG lipase AtDESL (Kim et al, 2011), and a number of MAG lipases (Kim et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the enzymatic activity and physiological function of the lipid droplet‐associated triacylglycerol lipase AtOBL1

Müller¹,

Ischebeck²

2017

New Phytologist

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Similar to seeds, pollen tubes contain lipid droplets that store triacylglycerol (TAG), but the fate of this TAG as well as the enzymes involved in its breakdown are unknown. Therefore, two potential TAG lipases from tobacco and Arabidopsis, NtOBL1 (Oil body lipase 1) and AtOBL1, were investigated, especially with respect to their importance for pollen tube growth. We expressed NtOBL1 and AtOBL1 as fluorescent fusion proteins to study their localization by confocal microscopy. Furthermore, we overexpressed AtOBL1 in Nicotiana benthamiana leaves to characterize it enzymatically. The obl1 mutant was studied in respect to its pollen tube growth in vivo and its seed germination. Both NtOBL1 and AtOBL1 localized to lipid droplets. AtOBL1 was abundant in pollen tubes and seedlings, and acted as a lipase on TAG, diacylglycerol and 1-monoacylglycerol at a pH optimum of 5.5. The obl1 mutant was hampered in pollen tube growth, whereas seedling establishment was not affected under optimal conditions, even though AtOBL1 accounted for a major lipase activity in seeds. TAG could be a direct precursor for the synthesis of membrane lipids in pollen tubes and proteins of the OBL family involved in the flux of acyl groups.

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Section: Introductionmentioning

confidence: 99%

Characterization of the enzymatic activity and physiological function of the lipid droplet‐associated triacylglycerol lipase AtOBL1

Müller¹,

Ischebeck²

2017

New Phytologist

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“…Instead, soluble MAGL might have contributed to the hydrolysis activity of NBD‐MAG in the present study. Some of the MAGL displayed hydrolysis activity with lysoPtdCho and lysophosphatidylethanolamine (lysoPtdEtn) in plant, Arabidopsis thaliana (Kim, Kim, Shim, & Suh, ). However, MAGL purified from adipose tissue of rat did not show any lysophospholipase activity for lysoPtdCho (Tornqvist & Belfrage, ).…”

Section: Discussionmentioning

confidence: 99%

Hydrolysis Activity of Pyloric Cecal Enterocytes of Brown Trout (Salmo trutta) toward Monoacylglycerol and Lysophosphatidylcholine

Egelandsdal

Olsen

2018

Lipids

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Some lipid digestion pathways in fish deviate from those in mammals, and many differences may also be species dependent. This report describes a pathway for monoacylglycerol (MAG) and lysophospholipid absorption by intestinal enterocytes in brown trout that may be of significance in salmonids. When culturing primary cells in a medium containing 1- and 2-MAG, we observed a massive hydrolysis of unesterified fatty acids. The hydrolysis activity was retained in the medium even after the removal of the cells. To further characterize these activities, both extracellular and isolated membrane proteins were tested for lipase activity toward triacylglycerol (TAG), diacylglycerol (DAG), MAG, phosphatidylcholine (PtdCho), and lysoPtdCho. In both cases, the main hydrolyzing activity was toward MAG followed by lysoPtdCho with very little activity toward DAG, TAG, or PtdCho. The extracellular and membrane proteins were partially purified by fast protein liquid chromatography and identified by proteomics (liquid chromatography-tandem mass spectrometry) focusing on lipase/hydrolase enzymes. In the membrane protein fraction, the data suggested that MAG was produced as an intermediate in the hydrolysis of lysoPtdCho by either lysophospholipase C or lysophospholipase D activity. Both abhydrolase-domain-containing protein 6 and abhydrolase-domain-containing protein 12 were identified in the membrane protein and they could be responsible for the hydrolysis of MAG. In the culture medium, low-peptide matches were found for ABHD6 and phospholipases and further studies are needed. In summary, trout enterocytes are capable of hydrolyzing MAG and lysoPtdCho. The enzymes are both extracellular and membrane bound. The pathways may be of significance during lipid absorption in fish lacking a 1,3 specific pancreatic lipase.

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“…Complete liberation of two fatty acids from the diacylglycerol moiety requires diacylglycerol lipase and monoacylglycerol lipase. The monoacylglycerol lipase was identified recently as MAGL8 (Kim et al, 2016b). The diacylglycerol lipase remains to be identified.…”

Section: Physical Interaction Between Oil Bodies and Glyoxysomes In Hmentioning

confidence: 99%

Membrane Dynamics and Multiple Functions of Oil Bodies in Seeds and Leaves

2017

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Molecular and biochemical characterizations of the monoacylglycerol lipase gene family of Arabidopsis thaliana

Cited by 56 publications

References 67 publications

Characterization of the enzymatic activity and physiological function of the lipid droplet‐associated triacylglycerol lipase AtOBL1

Characterization of the enzymatic activity and physiological function of the lipid droplet‐associated triacylglycerol lipase AtOBL1

Hydrolysis Activity of Pyloric Cecal Enterocytes of Brown Trout (Salmo trutta) toward Monoacylglycerol and Lysophosphatidylcholine

Membrane Dynamics and Multiple Functions of Oil Bodies in Seeds and Leaves

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