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Insights into membrane association of the SMP domain of extended synaptotagmin.
Nat Commun
March 2023
State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Frontiers Science Center for Cell Responses, Nankai University, Tianjin, China.
The Synaptotagmin-like Mitochondrial-lipid-binding Protein (SMP) domain is a newly identified lipid transfer module present in proteins that regulate lipid homeostasis at membrane contact sites (MCSs). However, how the SMP domain associates with the membrane to extract and unload lipids is unclear. Here, we performed in vitro DNA brick-assisted lipid transfer assays and in silico molecular dynamics simulations to investigate the molecular basis of the membrane association by the SMP domain of extended synaptotagmin (E-Syt), which tethers the tubular endoplasmic reticulum (ER) to the plasma membrane (PM).
View Article and Find Full Text PDFConformation-Dependent Human p52Shc Phosphorylation by Human c-Src.
Biochemistry
June 2015
†Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States.
Phosphorylation of the human p52Shc adaptor protein is a key determinant in modulating signaling complex assembly in response to tyrosine kinase signaling cascade activation. The underlying mechanisms that govern p52Shc phosphorylation status are unknown. In this study, p52Shc phosphorylation by human c-Src was investigated using purified proteins to define mechanisms that affect the p52Shc phosphorylation state.
View Article and Find Full Text PDFRelease of 11-cis-retinal from cellular retinaldehyde-binding protein by acidic lipids.
Mol Vis
August 2009
Department of Ophthalmology, University of Washington, School of Medicine, Seattle, WA 98195-6485, USA.
Purpose: To determine molecular mechanisms for the release of 11-cis-retinal from the binding pocket of cellular retinaldehyde-binding protein (CRALBP).
Methods: Binding of CRALBP to lipid surfaces was assessed with a lipid-immunoblot assay. Lipids were presented to CRALBP as small unilamellar vesicles (SUVs) consisting of phosphatidylcholine (PC) plus other lipids.
Molecular dynamics simulations of lung surfactant lipid monolayers.
Biophys Chem
December 2008
Department of Biochemistry, Memorial University of Newfoundland, Canada A1B 3X9.
Pulmonary surfactant provides for a lipid rich film at the lung air-water interface, which prevents alveolar collapse at the end of expiration. The films are likely enriched in the major surfactant component dipalmitoylphosphatidylcholine (DPPC), which, due to its saturated fatty acid chains, can withstand high surface pressures up to 70 mN/m, thereby reducing surface tension in that interface to very low values (close to 1 mN/m). Despite many experimental measurements in situ, as well as in vitro for native lung surfactant films, the exact mechanism by which other fluid lipid components of surfactant, in combination with surfactant proteins, allow for such low surface tension values to be reached is not well understood.
View Article and Find Full Text PDFChange in the concentration of neutrophil elastase in bronchoalveolar lavage fluid during anesthesia and its inhibition by cholesterol sulfate.
Transl Res
August 2006
Department of Anesthesiology, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.
Unlabelled: Cholesterol sulfate (CS) in the gastrointestinal tract exhibits a mucosal protective activity in mouse ulcer model. To clarify the possible role of CS for protection from the epithelial injury due to neutrophil elastase in the tracheobronchi, the authors determined the concentrations of CS and neutrophil elastase in bronchoalveolar lavage fluid (BALF) from patients under anesthesia, and they examined the inhibitory activity of CS toward neutrophil elastase. The concentrations of CS and neutrophil elastase were determined by thin-layer chromatography and enzyme-linked immunosorbent assaying, respectively, and the effect of CS on the activity of elastase was determined with a chromogenic substrate.
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