Structural insights into phospholipase D function. (January 2021)

• Record Type: Journal Article
• Authors: Yao, Yuanfa; Li, Jianxu; Lin, Yinyan; Zhou, Jiaqiang; Zhang, Peng; Xu, Yingke
• Is Part Of: Progress in lipid research. Volume 81(2021)
• Publication Date: 2021-01
• Subjects: AAs amino acids -- CDC42 cell division control protein 42 homolog -- CL cardiolipin -- DAG diacylglycerol -- Deptor DEP domain-containing mTOR-interacting protein -- DOCK2 dedicator of cytokinesis 2 -- ECM extracellular matrix -- EGF epidermal growth factor -- eNOS endothelial nitric oxide synthase -- FKBP38 prolyl-isomerase FK506-binding protein of 38 kDa -- EMT epithelial-to-mesenchymal transition -- GEF guanine nucleotide exchange factor -- Grb2 growth factor receptor-bound protein 2 -- HKD motif His(x)Lys(x)4Asp residues (x refers to any amino acid residue) -- hVps34 human vacuolar protein sorting 34 -- LRS leucyl tRNA synthetase -- MMP metalloproteinase -- mTOR mammalian target of rapamycin -- Nuc endonuclease -- NAPE N-acylphosphatidylethanolamine -- PA phosphatidic acid -- PC phosphatidylcholine -- PE phosphatidylethanolamine -- PG phosphatidylglycerol -- PS phosphatidylserine -- PIP2 phosphatidylinositol (4, 5)-bisphosphate -- PI(3)P phosphatidylinositol-3-phosphate -- PDGF platelet-derived growth factor -- PH pleckstrin-homology -- PX phox-homology -- piRNA P-element-induced wimpy testis (PIWI)-interacting RNA -- PI3K phosphoinositide 3-kinase -- PKC protein kinase C -- PLD phospholipase D -- PLDPMF PLD from Streptomyces sp. strain PMF -- Rac ras-related C3 botulinum toxin substrate -- RhoA rat sarcoma homolog family member A -- ROS reactive oxygen species -- RTK receptor tyrosine kinase -- RX3R motif Arg(x)3Arg residues -- SH2 src homology 2 -- SPO14 yeast PLD -- TCF-4 transcription factor 4 -- VEGFs vascular endothelial growth factors -- WASP Wiscott–Aldrich syndrome protein; Phospholipase D -- Phosphatidic acid -- Crystal structure -- HKD domain; Lipids -- Periodicals; Lipids -- Periodicals; Lipides -- Périodiques; Lipiden; 572.57
• DOI: 10.1016/j.plipres.2020.101070
• Languages: English
• ISSNs: 0163-7827

Abstract

Abstract: Phospholipase D (PLD) and its metabolic active product phosphatidic acid (PA) engage in a wide range of physiopathologic processes in the cell. PLDs have been considered as a potential and promising drug target. Recently, the crystal structures of PLDs in mammalian and plant have been solved at atomic resolution. These achievements allow us to understand the structural differences among different species of PLDs and the functions of their key domains. In this review, we summarize the sequence and structure of different species of PLD isoforms, and discuss the structural mechanisms for PLD interactions with their binding partners and the functions of each key domain in the regulation of PLDs activation and catalytic reaction. Graphical abstract: Unlabelled Image