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Cited by 228Lipid metabolism and biosynthesisPlant Molecular Biology ResearchSphingolipid Metabolism and Signaling

The DOI matches its Crossref record; 153 of the 153 references it cites were found in a registry or an index.

Function and regulation of phospholipid signalling in plants

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Xue, Hong-Wei, Chen, Xu, Mei, Yu·2009·Biochemical Journal
DOI 10.1042/bj20090300PMC PMC2708932
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Abstract

As an important metabolic pathway, phosphatidylinositol metabolism generates both constitutive and signalling molecules that are crucial for plant growth and development. Recent studies using genetic and molecular approaches reveal the important roles of phospholipid molecules and signalling in multiple processes of higher plants, including root growth, pollen and vascular development, hormone effects and cell responses to environmental stimuli plants. The present review summarizes the current progress in our understanding of the functional mechanism of phospholipid signalling, with an emphasis on the regulation of Ins(1,4,5)P3–Ca2+ oscillation, the second messenger molecule phosphatidic acid and the cytoskeleton.

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Crossref · 10.1042/bj20090300

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Figures

Figure 1 The phosphoinositide metabolic pathway in higher plants The isoform numbers of the key enzymes in Arabidopsis (At) and rice are indicated. Abbreviations: PI, phosphoinositide; PI5K, phosphoinositide 5-kinase.
Figure 1 The phosphoinositide metabolic pathway in higher plants The isoform numbers of the key enzymes in Arabidopsis (At) and rice are indicated. Abbreviations: PI, phosphoinositide; PI5K, phosphoinositide 5-kinase.CC BY-NC · PubMed Central
Figure 2 PA functions in hormone responses and growth of roots, root hairs and pollen tubes PA accumulates in response to treatment with auxin and NO, wounding, freezing, nutrient starvation, elicitor, xylanase, and osmotic stress. PA could bind CTR1 and block the interaction with ethylene receptor ETR1 to regulate the ethylene response. PA binds and decreases the activity of ABI1, resulting in the insensitive response to ABA treatment. PA promotes actin polymerization by binding to and inhibiting the activity of AtCP. PA regulates cycling of PIN proteins through directly mediating vesicle trafficking, or binding and mediating the activity of auxin transport upstream proteins PDK1, PINOID and PP2A. Abbreviations: CTR1-K, CTR1 kinase domain; PH, pleckstrin homology domain.
Figure 2 PA functions in hormone responses and growth of roots, root hairs and pollen tubes PA accumulates in response to treatment with auxin and NO, wounding, freezing, nutrient starvation, elicitor, xylanase, and osmotic stress. PA could bind CTR1 and block the interaction with ethylene receptor ETR1 to regulate the ethylene response. PA binds and decreases the activity of ABI1, resulting in the insensitive response to ABA treatment. PA promotes actin polymerization by binding to and inhibiting the activity of AtCP. PA regulates cycling of PIN proteins through directly mediating vesicle trafficking, or binding and mediating the activity of auxin transport upstream proteins PDK1, PINOID and PP2A. Abbreviations: CTR1-K, CTR1 kinase domain; PH, pleckstrin homology domain.CC BY-NC · PubMed Central
Figure 3 The Ca2+ oscillation, mediated by PtdIns(4,5)P2 and Ins(1,4,5)P3, is crucial for multiple processes of plant growth including root tropism, root hair formation, cotyledon vein development, photomorphogenesis, guard cell closure, pollen tube elongation and hormone effects
Figure 3 The Ca2+ oscillation, mediated by PtdIns(4,5)P2 and Ins(1,4,5)P3, is crucial for multiple processes of plant growth including root tropism, root hair formation, cotyledon vein development, photomorphogenesis, guard cell closure, pollen tube elongation and hormone effectsCC BY-NC · PubMed Central
Figure 4 Phospholipids participate in the tip growth of the root hair and pollen tube through regulating actin and microtubule cytoskeletons PtdIns(4,5)P2 is synthesized on the plasma membrane and assembles a number of endocytic accessory proteins to induce the antigen-stimulated endocytosis. PIP5K1 and PtdIns(4,5)P2 interact directly with actin and recruit PI4Kβ1 to actin. PtdIns(4,5)P2 interacts and suppresses the activity of actin-binding proteins, including severing proteins, capping proteins, ABPs (actin-binding proteins: fimbrin, villin, profilin), and induces the activity of α-actin to regulate actin remodelling. PA turnover from DAG is the substrate for PLD which is involved in microtubule reorganization. Ins(1,4,5)P3–Ca2+ oscillation regulates the activity of actin-binding proteins to participate in actin remodelling. Abbreviations: PC, phosphatidylcholine; PE, phosphatidylethanolamine.
Figure 4 Phospholipids participate in the tip growth of the root hair and pollen tube through regulating actin and microtubule cytoskeletons PtdIns(4,5)P2 is synthesized on the plasma membrane and assembles a number of endocytic accessory proteins to induce the antigen-stimulated endocytosis. PIP5K1 and PtdIns(4,5)P2 interact directly with actin and recruit PI4Kβ1 to actin. PtdIns(4,5)P2 interacts and suppresses the activity of actin-binding proteins, including severing proteins, capping proteins, ABPs (actin-binding proteins: fimbrin, villin, profilin), and induces the activity of α-actin to regulate actin remodelling. PA turnover from DAG is the substrate for PLD which is involved in microtubule reorganization. Ins(1,4,5)P3–Ca2+ oscillation regulates the activity of actin-binding proteins to participate in actin remodelling. Abbreviations: PC, phosphatidylcholine; PE, phosphatidylethanolamine.CC BY-NC · PubMed Central

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Research works printed but not linked: 1

  1. Li, 2004, The plasma membrane bound phospholipase Dδ enhances freezing tolerance in Arabidopsis thaliana, Nat. Biotechnol., 22, 427, 10.1038/nbt949 · DOI

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Metadata

Authors
Xue, H.-W., Chen, X., & Mei, Y.
Affiliations
  • Chinese Academy of Sciences (CN)
  • National Key Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 300 Fenglin Road, Shanghai 200032, China
Corresponding author
Xue, Hong-Wei
ORCID
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2009-06-26
Volume
421
Issue
2
Pages
145-156
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj20090300
PMC
PMC2708932
OpenAlex
W2066892182
Cited by
219
References
151
Citations by year
2026: 4 · 2025: 5 · 2024: 14 · 2023: 10 · 2022: 16 · 2021: 17 · 2020: 22 · 2019: 17 · 2018: 13 · 2017: 10 · 2016: 12 · 2015: 13 · 2014: 15 · 2013: 17 · 2012: 15
FWCI
0.88
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical Journal (publishedVersion, cc-by-nc)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Keywords
phosphoinositide metabolism, inositol 1,4,5-trisphosphate, calcium oscillations, phosphatidic acid, second messengers, cytoskeleton, root growth, pollen development, vascular development, plant hormone signaling, environmental stress response, plant growth and development
MeSH terms
Calcium, Inositol Phosphates, Models, Biological, Phosphatidylinositols, Phospholipids, Plant Proteins, Plants, Signal Transduction, Oxidative Stress, Gene Expression Regulation, Plant, Plant Roots

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