ArticleMolecular biology of the cell2007
Conformational dynamics of the major yeast phosphatidylinositol transfer protein sec14p: insight into the mechanisms of phospholipid exchange and diseases of sec14p-like protein deficiencies.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- The molecular mechanisms of visual chromophore release from cellular retinaldehyde-binding protein.Structure (London, England : 1993) · 2025Article
- A brief history of phosphatidylinositol transfer proteins: from the backwaters of cell biology to prime time in lipid signaling.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.PLoS biology · 2024Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- MOSPD2 is an endoplasmic reticulum-lipid droplet tether functioning in LD homeostasis.The Journal of cell biology · 2022Article
- Molecular Dynamics Simulations Reveal Structural Interconnections within Sec14-PH Bipartite Domain from Human Neurofibromin.International journal of molecular sciences · 2022Article
- Ceramide-1-phosphate transfer protein promotes sphingolipid reorientation needed for binding during membrane interaction.Journal of lipid research · 2022Article
- Emerging Prospects for Combating Fungal Infections by Targeting Phosphatidylinositol Transfer Proteins.International journal of molecular sciences · 2021Review
- A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins.eLife · 2020Article
- The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes.Journal of lipid research · 2019Review
- Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.Nature reviews. Molecular cell biology · 2019Review
- Biophysical Parameters of the Sec14 Phospholipid Exchange Cycle.Biophysical journal · 2019Article
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- Target Identification and Mechanism of Action of Picolinamide and Benzamide Chemotypes with Antifungal Properties.Cell chemical biology · 2018Article
- Tubular lipid binding proteins (TULIPs) growing everywhere.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Dynamics and energetics of the mammalian phosphatidylinositol transfer protein phospholipid exchange cycle.The Journal of biological chemistry · 2017Article
- Sec14-like phosphatidylinositol transfer proteins and the biological landscape of phosphoinositide signaling in plants.Biochimica et biophysica acta · 2016Review
- Phosphatidylinositol transfer proteins and instructive regulation of lipid kinase biology.Biochimica et biophysica acta · 2015Review
- Sec14-like phosphatidylinositol-transfer proteins and diversification of phosphoinositide signalling outcomes.Biochemical Society transactions · 2014Article
- PITPs as targets for selectively interfering with phosphoinositide signaling in cells.Nature chemical biology · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Molecular dynamics simulations coupled with functional analyses of the major yeast phosphatidylinositol/phosphatidylcholine transfer protein Sec14p identify structural elements involved in regulating the ability of Sec14p to execute phospholipid exchange. The molecular dynamics simulations suggest large rigid body motions within the Sec14p molecule accompany closing and opening of an A(10)/T(4)/A(11) helical gate, and that "state-of-closure" of this helical gate determines access to the Sec14p phospholipid binding cavity. The data also project that conformational dynamics of the helical gate are controlled by a hinge unit (residues F(212), Y(213), K(239), I(240), and I(242)) that links to the N- and C-terminal ends of the helical gate, and by a novel gating module (composed of the B(1)LB(2) and A(12)LT(5) substructures) through which conformational information is transduced to the hinge. The (114)TDKDGR(119) motif of B(1)LB(2) plays an important role in that transduction process. These simulations offer new mechanistic possibilities for an important half-reaction of the Sec14p phospholipid exchange cycle that occurs on membrane surfaces after Sec14p has ejected bound ligand, and is reloading with another phospholipid molecule. These conformational transitions further suggest structural rationales for known disease missense mutations that functionally compromise mammalian members of the Sec14-protein superfamily.
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