PHOSPHOINOSITIDE LIPIDS AS SIGNALING MOLECULES: Common Themes for Signal Transduction, Cytoskeletal Regulation, and Membrane Trafficking
Abstract
Signaling roles for phosphoinositides that involve their regulated hydrolysis to generate second messengers have been well characterized. Recent work has revealed additional signaling roles for phosphoinositides that do not involve their hydrolysis. PtdIns 3-P, PtdIns 3,4,5-P3, and PtdIns 4,5-P2 function as site-specific signals on membranes that recruit and/or activate proteins for the assembly of spatially localized functional complexes. A large number of phosphoinositide-binding proteins have been identified as the potential effectors for phosphoinositide signals. Common themes of localized signal generation and the spatially localized recruitment of effector proteins appear to underlie mechanisms employed in signal transduction, cytoskeletal, and membrane trafficking events.
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4,5-PIP2 is thought to govern the distribution and function of cytoskeletal and signaling proteins bearing pleckstrin homology domains or lysine/arginine-rich hydrophobic motifs that interact directly and specifically with its headgroup.
“This phospholipid is thought to govern the distribution and function of a variety of cytoskeletal and signaling proteins that bear pleckstrin homology (PH) domains or lysine/arginine-rich hydrophobic motifs, which interact directly and specifically with the headgroup of 4,5-PIP2 (Bottomley et al. 1998; Hinchliffe et al. 1998; Martin 1998; Czech 2000).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Martin 1998
Cites
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Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
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“This phospholipid is thought to govern the distribution and function of a variety of cytoskeletal and signaling proteins that bear pleckstrin homology (PH) domains or lysine/arginine-rich hydrophobic motifs, which interact directly and specifically with the headgroup of 4,5-PIP 2 (Bottomley et al., 1998; Hinchliffe et…”
BackgroundInfluentialDriving the cell cycle through metabolism
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A PTEN-related 5-Phosphatidylinositol Phosphatase Localized in the Golgi
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- Authors
- Martin, T. F. J.
- Affiliations
- University of Wisconsin–Madison (US)
- Corresponding author
- Martin, T. F. J.
- ORCID
- Martin, T. F. J.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 1998-11
- Volume
- 14
- Issue
- 1
- Pages
- 231-264
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2120077272
- Cited by
- 522
- References
- 2
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 4 · 2023: 3 · 2022: 6 · 2021: 10 · 2020: 13 · 2019: 13 · 2018: 3 · 2017: 8 · 2016: 7 · 2015: 10 · 2014: 10 · 2013: 5 · 2012: 16
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- phosphoinositides, phosphoinositide signaling, PtdIns(3)P, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphoinositide-binding proteins, signal transduction, cytoskeleton regulation, membrane trafficking
- MeSH terms
- Animals, Cell Membrane, Cytoskeleton, Humans, Membrane Fusion, Membrane Proteins, Phosphatidylinositols, Phosphorylation, Protein Kinases, Signal Transduction
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