Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions

被引：2

作者：

Stukey, Geordan J. ^{[1
,2
]}

Han, Gil-Soo ^{[1
,2
]}

Carman, George M. ^{[1
,2
]}

机构：

[1] Rutgers State Univ, Dept Food Sci, New Brunswick, NJ 08901 USA

[2] Rutgers State Univ, Rutgers Ctr Lipid Res, New Brunswick, NJ 08901 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2024年 / 1869卷 / 08期

基金：

美国国家卫生研究院;

关键词：

Diacylglycerol; Lipin; Pah1; Phosphatidic acid; Phospholipid; Phosphorylation; Protein kinase; Protein phosphatase; Triacylglycerol; Yeast; PROTEIN-KINASE-A; SACCHAROMYCES-CEREVISIAE; ACID-PHOSPHATASE; PHOSPHOLIPID-SYNTHESIS; LIPIN; PHOSPHOSERINE PHOSPHATASE; ENDOPLASMIC-RETICULUM; PHOSPHORYLATION SITES; MEMBRANE BIOGENESIS; CRYSTAL-STRUCTURE;

D O I：

10.1016/j.bbalip.2024.159547

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphatidate (PA) phosphatase, which catalyzes the Mg2+-dependent 2 +-dependent dephosphorylation of PA to produce diacylglycerol, provides a direct precursor for the synthesis of the storage lipid triacylglycerol and the membrane phospholipids phosphatidylcholine and phosphatidylethanolamine. The enzyme controlling the key phospholipid PA also plays a crucial role in diverse aspects of lipid metabolism and cell physiology. PA phosphatase is a peripheral membrane enzyme that is composed of multiple domains/regions required for its catalytic function and subcellular localization. In this review, we discuss the domains/regions of PA phosphatase from the yeast Saccharomyces cerevisiae with reference to the homologous enzyme from mammalian cells.

引用

页数：12

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