The functions of phospholipases and their hydrolysis products in plant growth, development and stress responses. (April 2022)
- Record Type:
- Journal Article
- Title:
- The functions of phospholipases and their hydrolysis products in plant growth, development and stress responses. (April 2022)
- Main Title:
- The functions of phospholipases and their hydrolysis products in plant growth, development and stress responses
- Authors:
- Ali, Usman
Lu, Shaoping
Fadlalla, Tarig
Iqbal, Sidra
Yue, Hong
Yang, Bao
Hong, Yueyun
Wang, Xuemin
Guo, Liang - Abstract:
- Abstract: Cell membranes are the initial site of stimulus perception from environment and phospholipids are the basic and important components of cell membranes. Phospholipases hydrolyze membrane lipids to generate various cellular mediators. These phospholipase-derived products, such as diacylglycerol, phosphatidic acid, inositol phosphates, lysophopsholipids, and free fatty acids, act as second messengers, playing vital roles in signal transduction during plant growth, development, and stress responses. This review focuses on the structure, substrate specificities, reaction requirements, and acting mechanism of several phospholipase families. It will discuss their functional significance in plant growth, development, and stress responses. In addition, it will highlight some critical knowledge gaps in the action mechanism, metabolic and signaling roles of these phospholipases and their products in the context of plant growth, development and stress responses.
- Is Part Of:
- Progress in lipid research. Volume 86(2022)
- Journal:
- Progress in lipid research
- Issue:
- Volume 86(2022)
- Issue Display:
- Volume 86, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 86
- Issue:
- 2022
- Issue Sort Value:
- 2022-0086-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-04
- Subjects:
- Phospholipases -- Phospholipid -- Diacylglycerol -- Free fatty acids -- Phosphatidic acid -- Signaling -- Stress response
FFA free fatty acid -- PA phosphatidic acid -- DAG diacylglycerol -- PLA phospholipase A -- PLC phospholipase C -- PLD phospholipase D -- pPLA patatin-related PLA -- sPLA2 secretory PLA2 -- iPLA2 calcium-independent PLA2 -- cPLAs calcium dependent PLAs -- PAF-AHS platelet-activating factor-acetyl hydrolases -- AdPLA adipose PLA -- NPC nonspecific phospholipase C -- PI-PLC phosphatidylinositol-specific PLC -- TAG triacylglycerol -- PC phosphatidylcholine -- MGDG monogalactosyldiacylglycerol -- DGDG digalactosyldiacylglycerol -- PG phosphatidyl glycerol -- GIPC glucosylinositolphosphorylceramide -- JA jasmonic acid -- ABA abscisic acid -- MTL matrilineal -- NLD not like dad -- GA gibberellic acid -- LPA lysophosphatidic acid -- LPC lysophosphatidycholine -- LPCAT1 lysophosphatidylcholine acyltransferase 1 -- HFA hydroxy fatty acids -- CPK calcium dependent protein kinase -- MAPK mitogen activated protein kinase -- SOS salt overly sensitive -- LPE lysophosphatidyletholamine -- CHAPS 3-((3-cholamidopropyl) dimethylammonio)-1-propanesulfonate -- PAP phosphatidic acid phosphatase -- PKC protein kinase C -- LPP lipid phosphate phosphatase -- PMT1 phospho-base N-methyltransferase 1 -- IAA indole acetic acid -- BL brassinolide -- LRX2 leucine-rich repeat/extensin 2 -- PI(4, 5)P2 phosphatidylinositol 4, 5-bisphosphate -- IP3 inositol 1, 4, 5-trisphosphate -- PI(4)P phosphatidylinositol-4-phosphate -- PI phosphatidylinositol -- CaM calmodulin -- PH plekstrin homology -- PBR1 phosphatidylinositol 4, 5-bisphosphate PI(4, 5)P2 binding region -- MCK1 calcium/calmodulin-dependent protein kinase -- TIR1 transport inhibitor response -- RG1 rhamnogalacturonan I -- PGA polygalacturonic acid -- RD29B responsive to desiccation 29B -- ZAT10 salt tolerance zinc finger 10 -- FLS2 flagellin sensing 2 -- ABI1 ABA insensitive 1 -- GAPC glyceraldehyde-3-phosphate dehydrogenases -- BIR2 bak1-interacting receptor-like kinase 2 -- NADPH nicotinamide adenine dinucleotide phosphate -- SPHK sphingosine kinase -- WER werewolf
Lipids -- Periodicals
Lipids -- Periodicals
Lipides -- Périodiques
Lipiden
572.57 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01637827 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.plipres.2022.101158 ↗
- Languages:
- English
- ISSNs:
- 0163-7827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6868.640000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21596.xml