AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway

AGPATs (1-acylglycerol-3-phosphate O-acyltransferases) catalyze the acylation of lysophosphatidic acid to form phosphatidic acid (PA), a key step in the synthesis of all glycerolipids. Here, the authors show that AGPAT2 and CDP-DAG synthases (CDS1 and CDS2) form functional complexes that promote fur...

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Autores principales: Hoi Yin Mak, Qian Ouyang, Sergey Tumanov, Jiesi Xu, Ping Rong, Feitong Dong, Sin Man Lam, Xiaowei Wang, Ivan Lukmantara, Ximing Du, Mingming Gao, Andrew J. Brown, Xin Gong, Guanghou Shui, Roland Stocker, Xun Huang, Shuai Chen, Hongyuan Yang
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/f5314785099443818eeaa3ca9fffb125
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spelling oai:doaj.org-article:f5314785099443818eeaa3ca9fffb1252021-11-28T12:32:46ZAGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway10.1038/s41467-021-27279-42041-1723https://doaj.org/article/f5314785099443818eeaa3ca9fffb1252021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27279-4https://doaj.org/toc/2041-1723AGPATs (1-acylglycerol-3-phosphate O-acyltransferases) catalyze the acylation of lysophosphatidic acid to form phosphatidic acid (PA), a key step in the synthesis of all glycerolipids. Here, the authors show that AGPAT2 and CDP-DAG synthases (CDS1 and CDS2) form functional complexes that promote further conversion of PA along the CDP-DAG pathway of phospholipid synthesis.Hoi Yin MakQian OuyangSergey TumanovJiesi XuPing RongFeitong DongSin Man LamXiaowei WangIvan LukmantaraXiming DuMingming GaoAndrew J. BrownXin GongGuanghou ShuiRoland StockerXun HuangShuai ChenHongyuan YangNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Hoi Yin Mak
Qian Ouyang
Sergey Tumanov
Jiesi Xu
Ping Rong
Feitong Dong
Sin Man Lam
Xiaowei Wang
Ivan Lukmantara
Ximing Du
Mingming Gao
Andrew J. Brown
Xin Gong
Guanghou Shui
Roland Stocker
Xun Huang
Shuai Chen
Hongyuan Yang
AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
description AGPATs (1-acylglycerol-3-phosphate O-acyltransferases) catalyze the acylation of lysophosphatidic acid to form phosphatidic acid (PA), a key step in the synthesis of all glycerolipids. Here, the authors show that AGPAT2 and CDP-DAG synthases (CDS1 and CDS2) form functional complexes that promote further conversion of PA along the CDP-DAG pathway of phospholipid synthesis.
format article
author Hoi Yin Mak
Qian Ouyang
Sergey Tumanov
Jiesi Xu
Ping Rong
Feitong Dong
Sin Man Lam
Xiaowei Wang
Ivan Lukmantara
Ximing Du
Mingming Gao
Andrew J. Brown
Xin Gong
Guanghou Shui
Roland Stocker
Xun Huang
Shuai Chen
Hongyuan Yang
author_facet Hoi Yin Mak
Qian Ouyang
Sergey Tumanov
Jiesi Xu
Ping Rong
Feitong Dong
Sin Man Lam
Xiaowei Wang
Ivan Lukmantara
Ximing Du
Mingming Gao
Andrew J. Brown
Xin Gong
Guanghou Shui
Roland Stocker
Xun Huang
Shuai Chen
Hongyuan Yang
author_sort Hoi Yin Mak
title AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
title_short AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
title_full AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
title_fullStr AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
title_full_unstemmed AGPAT2 interaction with CDP-diacylglycerol synthases promotes the flux of fatty acids through the CDP-diacylglycerol pathway
title_sort agpat2 interaction with cdp-diacylglycerol synthases promotes the flux of fatty acids through the cdp-diacylglycerol pathway
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/f5314785099443818eeaa3ca9fffb125
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