ArticleStructure (London, England : 1993)2015
Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Two-step mechanism of Bruton's tyrosine kinase membrane recruitment and activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Binding orientation of weakly associating membrane peripheral proteins via membrane paramagnetic relaxation enhancement NMR.Communications chemistry · 2026Article
- Two-Step Mechanism of Bruton's Tyrosine Kinase Membrane Recruitment and Activation.bioRxiv : the preprint server for biology · 2025Article
- An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function.Nature communications · 2025Article
- Cooperativity of PIP2 and PS lipids modulates PH domain binding.Biophysical journal · 2025Article
- The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism.bioRxiv : the preprint server for biology · 2024Article
- Membranes are functionalized by a proteolipid code.BMC biology · 2024Article
- Article
- Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023Article
- Intrinsically disordered region of talin's FERM domain functions as an initial PIPBiophysical journal · 2023Article
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- Two cooperative binding sites sensitize PI(4,5)PScience advances · 2022Article
- Systematic simulation of the interactions of pleckstrin homology domains with membranes.Science advances · 2022Article
- Gradients of PI(4,5)PFrontiers in cell and developmental biology · 2022Article
- Structural basis for the association of PLEKHA7 with membrane-embedded phosphatidylinositol lipids.Structure (London, England : 1993) · 2021Article
- Flexible pivoting of dynamin pleckstrin homology domain catalyzes fission: insights into molecular degrees of freedom.Molecular biology of the cell · 2021Article
- Attracted to membranes: lipid-binding domains in plants.Plant physiology · 2021Article
- Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b.The EMBO journal · 2021Article
- Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1.Science advances · 2020Article
- The BAR domain of the Arf GTPase-activating protein ASAP1 directly binds actin filaments.The Journal of biological chemistry · 2020Article
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12 authors.
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Abstract
We have defined the molecular basis for association of the PH domain of the Arf GAP ASAP1 with phospholipid bilayers. Structures of the unliganded and dibutyryl PtdIns(4,5)P2-bound PH domain were solved. PtdIns(4,5)P2 made contact with both a canonical site (C site) and an atypical site (A site). We hypothesized cooperative binding of PtdIns(4,5)P2 to the C site and a nonspecific anionic phospholipid to the A site. PtdIns(4,5)P2 dependence of binding to large unilamellar vesicles and GAP activity was sigmoidal, consistent with cooperative sites. In contrast, PtdIns(4,5)P2 binding to the PH domain of PLC δ1 was hyperbolic. Mutation of amino acids in either the C or A site resulted in decreased PtdIns(4,5)P2-dependent binding to vesicles and decreased GAP activity. The results support the idea of cooperative phospholipid binding to the C and A sites of the PH domain of ASAP1. We propose that the mechanism underlies rapid switching between active and inactive ASAP1.
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