Sphingolipid management by an orchestra of lipid transfer proteins

2008 ◽  
Vol 389 (11) ◽  
Author(s):  
Sylvia Neumann ◽  
Gerrit van Meer
Keyword(s):  
Lipid Composition ◽  
Metabolic Enzymes ◽  
Eukaryotic Cells ◽  
Sphingolipid Metabolism ◽  
Lipid Research ◽  
Lipid Transfer ◽  
Membrane Composition ◽  
Lipid Transfer Proteins ◽  
Basic Principles ◽  
And Function

Abstract The various membranes in eukaryotic cells have unique lipid compositions. Despite important discoveries in lipid research over recent decades, the basic principles by which cells define their membrane compositions are essentially unknown. Cells must sense the concentration of each lipid, integrate such signals and regulate the activity of their metabolic enzymes and transport routes to dynamically meet their needs in terms of membrane composition. Sphingolipids constitute a lipid category that is essential for eukaryotic life and appears to be key to differences in lipid composition. Here we discuss recent findings that assign an important role to lipid transfer proteins in the regulation of sphingolipid metabolism, organization and function.

scholarly journals Non‐specific lipid‐transfer proteins: Allergen structure and function, cross‐reactivity, sensitization, and epidemiology

2021 ◽  
Vol 11 (3) ◽  
Author(s):  
Isabel J. Skypala ◽  
Ricardo Asero ◽  
Domingo Barber ◽  
Lorenzo Cecchi ◽  
Arazeli Diaz Perales ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Structure And Function ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Allergen Structure ◽  
And Function ◽  
Specific Lipid

scholarly journals Lipid transfer proteins: classification, nomenclature, structure, and function

Planta ◽  
2016 ◽  
Vol 244 (5) ◽  
pp. 971-997 ◽  
Author(s):  
Tiina A. Salminen ◽  
Kristina Blomqvist ◽  
Johan Edqvist
Keyword(s):  
Structure And Function ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
And Function ◽  
Proteins Classification

scholarly journals Molecular determinants of ER–Golgi contacts identified through a new FRET–FLIM system

2019 ◽  
Vol 218 (3) ◽  
pp. 1055-1065 ◽  
Author(s):  
Rossella Venditti ◽  
Laura Rita Rega ◽  
Maria Chiara Masone ◽  
Michele Santoro ◽  
Elena Polishchuk ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Lipid Composition ◽  
Mechanistic Study ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Transfer Protein ◽  
Contact Sites ◽  
Molecular Determinants ◽  
Redundant Role ◽  
Perinuclear Area

ER–TGN contact sites (ERTGoCS) have been visualized by electron microscopy, but their location in the crowded perinuclear area has hampered their analysis via optical microscopy as well as their mechanistic study. To overcome these limits we developed a FRET-based approach and screened several candidates to search for molecular determinants of the ERTGoCS. These included the ER membrane proteins VAPA and VAPB and lipid transfer proteins possessing dual (ER and TGN) targeting motifs that have been hypothesized to contribute to the maintenance of ERTGoCS, such as the ceramide transfer protein CERT and several members of the oxysterol binding proteins. We found that VAP proteins, OSBP1, ORP9, and ORP10 are required, with OSBP1 playing a redundant role with ORP9, which does not involve its lipid transfer activity, and ORP10 being required due to its ability to transfer phosphatidylserine to the TGN. Our results indicate that both structural tethers and a proper lipid composition are needed for ERTGoCS integrity.

The role of the phosphoinositides at the Golgi complex

2007 ◽  
Vol 74 ◽  
pp. 107-116 ◽  
Author(s):  
Maria Antonietta De Matteis ◽  
Giovanni D'Angelo
Keyword(s):  
Golgi Complex ◽  
Small Gtpases ◽  
Eukaryotic Cells ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Cell Organelles ◽  
Binding Domains ◽  
Ability To Act ◽  
Endocytic Pathways

Eukaryotic cells are organized into a complex system of subcompartments, each with its distinct protein and lipid composition. A continuous flux of membranes crosses these compartments, and in some cases direct connections exist between the different organelles. It is thus surprising that they can maintain their individual identities. Small GTPases and the phosphoinositides have emerged as the key regulators in the maintenance of the identity of the Golgi complex. This property is due to their ability to act either alone or, more often, in combination, as cues directing and controlling the recruitment of proteins that possess phosphoinositide-binding domains. Among these many proteins there are the lipid transfer proteins, which can transfer ceramide, oxysterol, cholesterol and possibly glucosylceramide. By regulating these lipid transfer proteins in this way, this binomial combination of the small GTPases and the phosphoinositides acquires a further important role: control of the synthesis and/or distribution of other important integral constituents of cell organelles, such as the sphingolipids and cholesterol. This role is particularly relevant at the level of the Golgi complex, a key organelle in the biosynthesis, transport and sorting of both lipids and proteins that is located at the intersection of the secretory and endocytic pathways.

scholarly journals ER-PM contacts regulate apical domain formation in hepatocytes

2020 ◽  
Author(s):  
Gary Hong Chun Chung ◽  
Jemima J. Burden ◽  
Maëlle Lorvellec ◽  
Paul Gissen ◽  
Christopher J. Stefan
Keyword(s):  
Basal Membrane ◽  
Small Gtpase ◽  
Cytoskeletal Proteins ◽  
Domain Formation ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Spatial Organisation ◽  
Apical Domain ◽  
Anionic Lipids ◽  
And Function

AbstractApico-basal membrane polarity is fundamental for epithelial cell development and function. Polarity factors including the small GTPase Cdc42, the Par3/Par6/aPKC complex, and cytoskeletal proteins are recruited by the anionic lipids phosphatidylinositol 4,5-bisphosphate and phosphatidylserine. But how these lipids accumulate at polarised sites remains unclear. We have examined roles of contacts between the endoplasmic reticulum and plasma membrane (ER-PM contacts) in generating lipid gradients during apical domain formation. Comprehensive electron microscopy analyses in hepatocytes and epithelial spheroids revealed two distinct ER-PM contact architectures that are spatially linked to apical and baso-lateral domains. Moreover, apical domain formation was delayed in HepG2 cells upon modulating the ER-PM contact proteins E-Syt1 and ORP5. We propose ER-PM contacts regulate apico-basal polarity via the lipid transfer proteins E-Syt1 and ORP5. Importantly, our findings suggest that the spatial organisation of ER-PM contacts is a conserved feature of polarised epithelial cells.

scholarly journals Sphingolipid Metabolism at the ER-Golgi Contact Zone and Its Impact on Membrane Trafficking

Contact ◽  
2020 ◽  
Vol 3 ◽  
pp. 251525642095951
Author(s):  
Asako Goto ◽  
Aya Mizuike ◽  
Kentaro Hanada
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Metabolism ◽  
Golgi Apparatus ◽  
Membrane Trafficking ◽  
Membrane Lipids ◽  
Sphingolipid Metabolism ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
Golgi Network ◽  
And Control

Proteins and lipids represent the two major constituents of biological membranes. Different organelles have different lipid compositions, which may be crucial for the execution and control of various organelle-specific functions. The interorganellar transport of lipids is dominated by mechanisms that are distinct from the vesicular mechanisms that underlie the interorganellar transport of proteins. Lipid transfer proteins (LTPs) efficiently and accurately mediate the trafficking of membrane lipids at the interfaces between different organelles. In this review, which focuses on sphingolipids, we describe the coordinated synthesis and transfer of lipids that occur at the endoplasmic reticulum (ER)-Golgi apparatus contact zones and discuss the impacts of lipid metabolism on membrane trafficking from the trans-Golgi network (TGN).

Lipid transfer proteins in Parietaria judaica L. pollen grains: immunocytochemical localization and function

2004 ◽  
Vol 83 (9) ◽  
pp. 493-497 ◽  
Author(s):  
Ana M. Vega-Maray ◽  
Delia Fernández-González ◽  
Rosa Valencia-Barrera ◽  
Florentino Polo ◽  
Juan A. Seoane-Camba ◽  
...  
Keyword(s):  
Pollen Grains ◽  
Immunocytochemical Localization ◽  
Lipid Transfer ◽  
Lipid Transfer Proteins ◽  
And Function
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