scholarly journals Dissecting the membrane lipid binding properties and lipase activity ofMycobacterium tuberculosisLipY domains

FEBS Journal ◽  
2019 ◽  
Vol 286 (16) ◽  
pp. 3164-3181 ◽  
Author(s):  
Pierre Santucci ◽  
Nabil Smichi ◽  
Sadia Diomandé ◽  
Isabelle Poncin ◽  
Vanessa Point ◽  
...  
Keyword(s):  
Lipase Activity ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Binding Properties

scholarly journals Triple-Knockout, Synuclein-Free Mice Display Compromised Lipid Pattern

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3078
Author(s):  
Irina A. Guschina ◽  
Natalia Ninkina ◽  
Andrei Roman ◽  
Mikhail V. Pokrovskiy ◽  
Vladimir L. Buchman
Keyword(s):  
Fatty Acids ◽  
Lipid Metabolism ◽  
Family Members ◽  
Ether Lipid ◽  
Brain Regions ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Synaptic Functions ◽  
Ethanolamine Plasmalogens ◽  
Lipid Pattern

Recent studies have implicated synucleins in several reactions during the biosynthesis of lipids and fatty acids in addition to their recognised role in membrane lipid binding and synaptic functions. These are among aspects of decreased synuclein functions that are still poorly acknowledged especially in regard to pathogenesis in Parkinson’s disease. Here, we aimed to add to existing knowledge of synuclein deficiency (i.e., the lack of all three family members), with respect to changes in fatty acids and lipids in plasma, liver, and two brain regions in triple synuclein-knockout (TKO) mice. We describe changes of long-chain polyunsaturated fatty acids (LCPUFA) and palmitic acid in liver and plasma, reduced triacylglycerol (TAG) accumulation in liver and non-esterified fatty acids in plasma of synuclein free mice. In midbrain, we observed counterbalanced changes in the relative concentrations of phosphatidylcholine (PC) and cerebrosides (CER). We also recorded a notable reduction in ethanolamine plasmalogens in the midbrain of synuclein free mice, which is an important finding since the abnormal ether lipid metabolism usually associated with neurological disorders. In summary, our data demonstrates that synuclein deficiency results in alterations of the PUFA synthesis, storage lipid accumulation in the liver, and the reduction of plasmalogens and CER, those polar lipids which are principal compounds of lipid rafts in many tissues. An ablation of all three synuclein family members causes more profound changes in lipid metabolism than changes previously shown to be associated with γ-synuclein deficiency alone. Possible mechanisms by which synuclein deficiency may govern the reported modifications of lipid metabolism in TKO mice are proposed and discussed.

Non enzymatic glycation of apolipoprotein A-I. Effects on its self-association and lipid binding properties

1988 ◽  
Vol 153 (3) ◽  
pp. 1060-1067 ◽  
Author(s):  
Carlos Calvo ◽  
Corinne Talussot ◽  
Gabriel Ponsin ◽  
Francois Berthézène
Keyword(s):  
Lipid Binding ◽  
Binding Properties ◽  
Apolipoprotein A ◽  
Self Association

Study of the relationship between lipid binding properties of cyclodextrins and their effect on the integrity of liposomes

2007 ◽  
Vol 338 (1-2) ◽  
pp. 35-42 ◽  
Author(s):  
G. Piel ◽  
M. Piette ◽  
V. Barillaro ◽  
D. Castagne ◽  
B. Evrard ◽  
...  
Keyword(s):  
Lipid Binding ◽  
Binding Properties ◽  
The Relationship

scholarly journals Isolation, Characterization and Lipid-Binding Properties of the Recalcitrant FtsA Division Protein from Escherichia coli

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39829 ◽  
Author(s):  
Ariadna Martos ◽  
Begoña Monterroso ◽  
Silvia Zorrilla ◽  
Belén Reija ◽  
Carlos Alfonso ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lipid Binding ◽  
Binding Properties

scholarly journals The structure and flexibility analysis of the Arabidopsis Synaptotagmin 1 reveal the basis of its regulation at membrane contact sites

2021 ◽  
Author(s):  
Juan Luis Benavente ◽  
Dritan Siliqi ◽  
Lourdes Infantes ◽  
Laura Lagartera ◽  
Alberto Mills ◽  
...  
Keyword(s):  
Cell Function ◽  
Lipid Extraction ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
C2 Domains ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Cellular Environment ◽  
Synaptotagmin 1

Cell function requires the maintenance of membrane lipid homeostasis as changes in cellular environment unbalance this equilibrium. The non-vesicular lipid transfer at endoplasmic reticulum (ER) and plasma membrane (PM) contact sites (CS) is central to restore it. Extended synaptotagmins (E-Syts) are ER proteins that play a central role in this process as they act as molecular tethers with PM and as lipid transfer proteins between these organelles. E-Syts are constitutively anchored to the ER through an N-terminal hydrophobic segment and bind to the PM via C-terminal C2 domains. In plants, synaptotagmins (SYTs) are orthologous of E-Syts and regulate the ER-PM communication by the activity of their two C2 domains in response to abiotic stresses. We have combined macromolecular crystallography, small-angle X-ray scattering, structural bioinformatics and biochemical data to analyze the regulation of plant synaptotagmin 1 (SYT1). Our data show that the binding of SYT1 to the PM is regulated by the interaction of the first C2 domain through a Ca2+-dependent lipid binding site and by a site for phosphorylated forms of phosphatidylinositol in such a way that two different molecular signals are integrated in response to stress. In addition, our data show that SYT1 is highly flexible by virtue of up to three hinge points, including one that connects the two C2 domains. This feature provides conformational freedom to SYT1 to define a large and complementary interaction surface with the PM. This structural plasticity, in turn, may facilitate lipid extraction, protein loading and subsequent transfer between PM and ER.

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