Tracking Diacylglycerol and Phosphatidic Acid Pools in Budding Yeast.

Lipid insights Pub Date : 2016-04-06 eCollection Date: 2015-01-01 DOI:10.4137/LPI.S31781
Suriakarthiga Ganesan, Brittney N Shabits, Vanina Zaremberg
{"title":"Tracking Diacylglycerol and Phosphatidic Acid Pools in Budding Yeast.","authors":"Suriakarthiga Ganesan,&nbsp;Brittney N Shabits,&nbsp;Vanina Zaremberg","doi":"10.4137/LPI.S31781","DOIUrl":null,"url":null,"abstract":"<p><p>Phosphatidic acid (PA) and diacylglycerol (DAG) are key signaling molecules and important precursors for the biosynthesis of all glycerolipids found in eukaryotes. Research conducted in the model organism Saccharomyces cerevisiae has been at the forefront of the identification of the enzymes involved in the metabolism and transport of PA and DAG. Both these lipids can alter the local physical properties of membranes by introducing negative curvature, but the anionic nature of the phosphomonoester headgroup in PA sets it apart from DAG. As a result, the mechanisms underlying PA and DAG interaction with other lipids and proteins are notoriously different. This is apparent from the analysis of the protein domains responsible for recognition and binding to each of these lipids. We review the current evidence obtained using the PA-binding proteins and domains fused to fluorescent proteins for in vivo tracking of PA pools in yeast. In addition, we present original results for visualization of DAG pools in yeast using the C1 domain from mammalian PKCδ. An emerging first cellular map of the distribution of PA and DAG pools in actively growing yeast is discussed. </p>","PeriodicalId":18039,"journal":{"name":"Lipid insights","volume":"8 Suppl 1","pages":"75-85"},"PeriodicalIF":0.0000,"publicationDate":"2016-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4137/LPI.S31781","citationCount":"20","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Lipid insights","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.4137/LPI.S31781","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2015/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 20

Abstract

Phosphatidic acid (PA) and diacylglycerol (DAG) are key signaling molecules and important precursors for the biosynthesis of all glycerolipids found in eukaryotes. Research conducted in the model organism Saccharomyces cerevisiae has been at the forefront of the identification of the enzymes involved in the metabolism and transport of PA and DAG. Both these lipids can alter the local physical properties of membranes by introducing negative curvature, but the anionic nature of the phosphomonoester headgroup in PA sets it apart from DAG. As a result, the mechanisms underlying PA and DAG interaction with other lipids and proteins are notoriously different. This is apparent from the analysis of the protein domains responsible for recognition and binding to each of these lipids. We review the current evidence obtained using the PA-binding proteins and domains fused to fluorescent proteins for in vivo tracking of PA pools in yeast. In addition, we present original results for visualization of DAG pools in yeast using the C1 domain from mammalian PKCδ. An emerging first cellular map of the distribution of PA and DAG pools in actively growing yeast is discussed.

Abstract Image

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
芽殖酵母中二酰基甘油和磷脂酸池的追踪。
磷脂酸(PA)和二酰基甘油(DAG)是真核生物合成所有甘油脂的关键信号分子和重要前体。在模式生物酿酒酵母中进行的研究一直处于鉴定参与PA和DAG代谢和运输的酶的前沿。这两种脂质都可以通过引入负曲率来改变膜的局部物理性质,但PA中磷酸单酯头基团的阴离子性质使其与DAG不同。因此,PA和DAG与其他脂质和蛋白质相互作用的机制是众所周知的不同。从负责识别和结合这些脂质的蛋白质结构域的分析中可以明显看出这一点。我们回顾了目前利用PA结合蛋白和融合荧光蛋白的结构域在酵母中追踪PA池的证据。此外,我们提出了利用哺乳动物PKCδ的C1结构域在酵母中可视化DAG池的原始结果。讨论了活跃生长酵母中PA和DAG池分布的新出现的第一张细胞图。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Effects of Phenylalanine on the Liquid-Expanded and Liquid-Condensed States of Phosphatidylcholine Monolayers. Cholesterol-Binding Sites in GIRK Channels: The Devil is in the Details. Some Lipid Droplets Are More Equal Than Others: Different Metabolic Lipid Droplet Pools in Hepatic Stellate Cells. Intracellular Lipid Droplets: From Structure to Function. Four Acyltransferases Uniquely Contribute to Phospholipid Heterogeneity in Saccharomyces cerevisiae
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1