ReviewThe Biochemical journal2000
Signal-dependent membrane targeting by pleckstrin homology (PH) domains.
Review in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers.
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Who cites it
253 citing papers in PubMed, 708 citations in OpenAlex.
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- Nanoscale clustering and dynamics of phosphatidylinositol 4,5-bisphosphate in an immune cell model.Biophysical journal · 2025Article
- PHLDA2 in cancer: From molecular mechanisms to therapeutic opportunities.The Journal of pharmacology and experimental therapeutics · 2025Review
- A Genome-Wide Modeling and Characterization Study of Pleckstrin Homology Domains inPlants (Basel, Switzerland) · 2025Article
- Identification of Houge type of X-linked syndromic mental retardation caused by CNKSR2 truncated variants.Italian journal of pediatrics · 2025Article
- Expansion of B10 cellsInternational journal of molecular medicine · 2025Review
- Conditional requirement for dimerization of the membrane-binding module for BTK signaling in lymphocyte cell lines.Science signaling · 2025Article
- Expanding on roles of pleckstrin homology-like domain family A member 1 protein.Cell and tissue research · 2025Review
- Small Molecule Modulator of the mTORC2 Pathway Discovered from a DEL Library Designed to Bind to Pleckstrin Homology Domains.ACS chemical biology · 2024Article
- Beyond biomarkers: Exploring the diverse potential of a novel phosphoprotein in lung cancer management.Journal of cellular and molecular medicine · 2024Review
- Evolution and screening of Trichoderma reesei mutants for secreted protein production at elevated temperature.Journal of industrial microbiology & biotechnology · 2024Article
- Phafins Are More Than Phosphoinositide-Binding Proteins.International journal of molecular sciences · 2023Review
- Mechanistic analysis of a novel membrane-interacting variable loop in the pleckstrin-homology domain critical for dynamin function.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- PI4P and BLOC-1 remodel endosomal membranes into tubules.The Journal of cell biology · 2022Article
- TDAG51-Deficiency Podocytes are Protected from High-Glucose-Induced Damage Through Nrf2 Activation via the AKT-GSK-3β Pathway.Inflammation · 2022Article
- Systematic simulation of the interactions of pleckstrin homology domains with membranes.Science advances · 2022Article
- Impact of CaBiomolecules · 2022Article
- Creativity comes from interactions: modules of protein interactions in plants.The FEBS journal · 2022Review
193 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Pleckstrin homology (PH) domains are small protein modules of around 120 amino acids found in many proteins involved in cell signalling, cytoskeletal rearrangement and other processes. Although several different protein ligands have been proposed for PH domains, their only clearly demonstrated physiological function to date is to bind membrane phosphoinositides. The PH domain from phospholipase C-delta(1) binds specifically to PtdIns(4,5)P(2) and its headgroup, and has become a valuable tool for studying cellular PtdIns(4,5)P(2) functions. More recent developments have demonstrated that a subset of PH domains recognizes the products of agonist-stimulated phosphoinositide 3-kinases. Fusion of these PH domains to green fluorescent protein has allowed dramatic demonstrations of their independent ability to drive signal-dependent recruitment of their host proteins to the plasma membrane. We discuss the structural basis for this 3-phosphoinoistide recognition and the role that it plays in cellular signalling. PH domains that bind specifically to phosphoinositides comprise only a minority (perhaps 15%) of those known, raising questions as to the physiological role of the remaining 85% of PH domains. Most (if not all) PH domains bind weakly and non-specifically to phosphoinositides. Studies of dynamin-1 have indicated that oligomerization of its PH domain may be important in driving membrane association. We discuss the possibility that membrane targeting by PH domains with low affinity for phosphoinositides could be driven by alteration of their oligomeric state and thus the avidity of their membrane binding.
Indexed as
Identifiers
10926821PMC1221219W2016441216What 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.