Mechanism of the phospholipid transfer protein-mediated transfer of phospholipids from model lipid vesicles to high density lipoproteins

Lalanne, Florent; Ponsin, Gabriel

doi:10.1016/s1388-1981(00)00087-1

Cited by 17 publications

(16 citation statements)

References 37 publications

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“…These in vitro studies suggest that LTPs markedly facilitate (several orders of magnitude) lipid transport between membranes, possibly by increasing the rate of lipid absorption from the bilayers (Lalanne and Ponsin 2000). Further structural, biochemical, and biophysical studies suggest that the lipid-transfer domain (LTD) of LTPs contains a hydrophobic lipid-binding tunnel that accommodates a single lipid molecule.…”

Section: Nonvesicular Lipid Transport By Ltpsmentioning

confidence: 91%

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Lev

2012

Cold Spring Harbor Perspectives in Biology

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Section: Nonvesicular Lipid Transport By Ltpsmentioning

confidence: 91%

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Lev

2012

Cold Spring Harbor Perspectives in Biology

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“…The ability of LTPs to mediate lipid transport between membranes was demonstrated in numerous in vitro studies using radiolabeled or fluorescent lipids [132]. This inter-membrane lipid transport is likely caused by LTPs binding and facilitating lipid desorption from membranes [133]. It was proposed that lipid transfer between membranes via LTPs in vivo would be most efficient when LTPs function at membrane contact sites where LTPs can simultaneously bind two membrane compartments (Figure 4A) [26, 132, 134, 135].…”

Section: Regulation Of Pi(45)p2 Homeostasis Via the Pi Cyclementioning

confidence: 99%

Homeostatic regulation of the PI(4,5)P 2 –Ca 2+ signaling system at ER–PM junctions

Chang

Liou

2016

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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The phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-Ca2+ signaling system is important for cell activation in response to various extracellular stimuli. This signaling system is initiated by receptor-induced hydrolysis of PI(4,5)P2 in the plasma membrane (PM) to generate the soluble second messenger inositol 1,4,5-trisphosphate (IP3). IP3 subsequently triggers the release of Ca2+ from the endoplasmic reticulum (ER) store to the cytosol to activate Ca2+-mediated responses, such as secretion and proliferation. The consumed PM PI(4,5)P2 and ER Ca2+ must be quickly restored to sustain signaling responses, and to maintain the homeostasis of PI(4,5)P2 and Ca2+. Since phosphatidylinositol (PI), the precursor lipid for PM PI(4,5)P2, is synthesized in the ER membrane, and a Ca2+ influx across the PM is required to refill the ER Ca2+ store, efficient communications between the ER and the PM are critical for the homeostatic regulation of the PI(4,5)P2-Ca2+ signaling system. This review describes the major findings that established the framework of the PI(4,5)P2-Ca2+ signaling system, and recent discoveries on feedback control mechanisms at ER-PM junctions that sustain the PI(4,5)P2-Ca2+ signaling system. Particular emphasis is placed on the characterization of ER-PM junctions where efficient communications between the ER and the PM occurs, and the activation mechanisms of proteins that dynamically localize to ER-PM junctions to provide the feedback control during PI(4,5)P2-Ca2+ signaling, including the ER Ca2+ sensor STIM1, the extended synaptotagmin E-Syt1, and the PI transfer protein Nir2. This review is part of a Special Issue entitled The Cellular Lipid Landscape.

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“…Models for phospholipid transfer proteins developed previously [51][52][53][54][55][56] generally relied on ordinary two substrate enzyme-catalyzed reactions that could be described by ping-pong BiBi mechanisms. While the models were well suited for transfer mechanisms involving single component lipid membranes, such as phosphatidylcholine transfer protein [51], with GLTP, a minor lipid component (e.g.…”

Section: Gltp Mechanism Of Actionmentioning

confidence: 99%

Glycolipid transfer proteins

Brown

Mattjus

2007

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Glycolipid transfer proteins (GLTPs) are small (24 kD), soluble, ubiquitous proteins characterized by their ability to accelerate the intermembrane transfer of glycolipids in vitro. GLTP specificity encompasses both sphingoid-and glycerol-based glycolipids, but with a strict requirement that the initial sugar residue be beta-linked to the hydrophobic lipid backbone. The 3D protein structures of GLTP reveal liganded structures with unique lipid binding modes. The biochemical properties of GLTP action at the membrane surface have been studied rather comprehensively, but the biological role of GLTP remains enigmatic. What is clear is that GLTP differs distinctly from other known glycolipid-binding proteins, such as nonspecific lipid transfer proteins, lysosomal sphingolipid activator proteins, lectins, lung surfactant proteins as well as other lipid binding/transfer proteins. Based on the unique conformational architecture that targets GLTP to membranes and enables glycolipid binding, GLTP is now considered the prototypical and founding member of a new protein superfamily in eukaryotes.

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Mechanism of the phospholipid transfer protein-mediated transfer of phospholipids from model lipid vesicles to high density lipoproteins

Cited by 17 publications

References 37 publications

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Homeostatic regulation of the PI(4,5)P 2 –Ca 2+ signaling system at ER–PM junctions

Glycolipid transfer proteins

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