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Cited by 101Protein Kinase Regulation and GTPase SignalingCellular Mechanics and InteractionsLipid Membrane Structure and Behavior

Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms

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Janmey, Paul A., Bucki, Robert, Radhakrishnan, Ravi·2018·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2018.07.155PMC PMC6269227
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Abstract

Actin cytoskeleton dynamics depend on a tight regulation of actin filament formation from an intracellular pool of monomers, followed by their linkage to each other or to cell membranes, followed by their depolymerization into a fresh pool of actin monomers. The ubiquitous requirement for continuous actin remodeling that is necessary for many cellular functions is orchestrated in large part by actin binding proteins whose affinity for actin is altered by inositol phospholipids, most prominently PI(4,5)P2 (phosphatidylinositol 4,5-bisphosphate). The kinetics of PI(4,5)P2 synthesis and hydrolysis, its lateral distribution within the lipid bilayer, and coincident detection of PI(4,5)P2 and another signal, all play a role in determining when and where a particular PI(4,5)P2-regulated protein is inactivated or activated to exert its effect on the actin cytoskeleton. This review summarizes a range of models that have been developed to explain how PI(4,5)P2 might function in the complex chemical and structural environment of the cell based on a combination of experiment and computational studies.

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  • PI(4,5)P2 is one of the main drivers of actin cytoskeleton remodelling; it interacts with several actin-binding proteins at the plasma membrane and regulates their activity through its levels.

    “One of the main drivers for this process is PI(4,5)P2 [87]; it interacts with several actin-binding proteins at the plasma membrane, serving to regulate their activity through its levels (Figure 5) [14,88].”

    From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [88]

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Authors
Janmey, P. A., Bucki, R., & Radhakrishnan, R.
Affiliations
  • University of Pennsylvania (US)
  • Medical University of Białystok (PL)
Corresponding author
Janmey, Paul A.
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2018-11
Volume
506
Issue
2
Pages
307-314
ISSN
0006-291X (ISSN-L)
DOI
10.1016/j.bbrc.2018.07.155
PMC
PMC6269227
OpenAlex
W2885287769
Cited by
101
References
0
Citations by year
2026: 4 · 2025: 13 · 2024: 8 · 2023: 11 · 2022: 21 · 2021: 11 · 2020: 25 · 2019: 5 · 2018: 3
FWCI
1.08
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochemical and Biophysical Research Communications (acceptedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • Narodowym Centrum Nauki (UMO-2015/17/B/NZ6/03473)
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 Mechanics and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords
actin cytoskeleton, actin polymerization, actin depolymerization, phosphatidylinositol 4,5-bisphosphate, inositol phospholipids, actin-binding proteins, lipid signaling, actin cytoskeleton remodeling, computational model
MeSH terms
Ezrin, Actins, Animals, Cell Membrane, Cytoskeletal Proteins, Eukaryotic Cells, Gene Expression Regulation, Humans, Kinetics, Microfilament Proteins, Actin Cytoskeleton, Models, Biological, Myosins, Osteochondrodysplasias, Xenopus laevis, Signal Transduction, Talin, Phosphatidylinositol 4,5-Diphosphate, Phospholipase C beta

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