ReviewAnnual review of physiology2015
Phosphoinositide control of membrane protein function: a frontier led by studies on ion channels.
Review in Annual review of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
62 citing papers in PubMed, 93 citations in OpenAlex.
- PIPbioRxiv : the preprint server for biology · 2026Article
- A new functional assay reveals that membrane binding is critical for overactivation of the phosphoinositide 3-kinase H1047R mutant.The Journal of biological chemistry · 2026Article
- Allosteric coupling between PIPProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Understanding Ion Channel Gating Mechanisms by Molecular Dynamics Simulations.Advances in experimental medicine and biology · 2026Review
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Inositol and PIP2/PIP3 Ratio: At the Crossroad of the Biodynamic Interface Between Cells and Their Microenvironment.Biomolecules · 2025Review
- Role for the PIPJournal of cell communication and signaling · 2024Review
- Structural basis of the activation of TRPV5 channels by long-chain acyl-Coenzyme-A.Nature communications · 2023Article
- PI(4,5)P2 regulates the gating of NaV1.4 channels.The Journal of general physiology · 2023Article
- PI(4,5)PAdvances in experimental medicine and biology · 2023Article
- RyR2 regulates store-operated Ca2+ entry, phospholipase C activity, and electrical excitability in the insulinoma cell line INS-1.PloS one · 2023Article
- Lipid-mediated prestin organization in outer hair cell membranes and its implications in sound amplification.Nature communications · 2022Article
- Hypoxia inhibits the cardiaciScience · 2022Article
- Use of a Molecular Switch Probe to Activate or Inhibit GIRK1 Heteromers In Silico Reveals a Novel Gating Mechanism.International journal of molecular sciences · 2022Article
- Inwardly rectifying KAmerican journal of physiology. Cell physiology · 2022Review
- Biophysical physiology of phosphoinositide rapid dynamics and regulation in living cells.The Journal of general physiology · 2022Article
- PKC regulation of ion channels: The involvement of PIPThe Journal of biological chemistry · 2022Review
- Correlation between structure and function in phosphatidylinositol lipid-dependent Kir2.2 gating.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- INPP5E controls ciliary localization of phospholipids and the odor response in olfactory sensory neurons.Journal of cell science · 2022Article
- G protein-coupled receptor-effector macromolecular membrane assemblies (GEMMAs).Pharmacology & therapeutics · 2022Review
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Anionic phospholipids are critical constituents of the inner leaflet of the plasma membrane, ensuring appropriate membrane topology of transmembrane proteins. Additionally, in eukaryotes, the negatively charged phosphoinositides serve as key signals not only through their hydrolysis products but also through direct control of transmembrane protein function. Direct phosphoinositide control of the activity of ion channels and transporters has been the most convincing case of the critical importance of phospholipid-protein interactions in the functional control of membrane proteins. Furthermore, second messengers, such as [Ca(2+)]i, or posttranslational modifications, such as phosphorylation, can directly or allosterically fine-tune phospholipid-protein interactions and modulate activity. Recent advances in structure determination of membrane proteins have allowed investigators to obtain complexes of ion channels with phosphoinositides and to use computational and experimental approaches to probe the dynamic mechanisms by which lipid-protein interactions control active and inactive protein states.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.