The orchestra of lipid-transfer proteins at the crossroads between metabolism and signaling. (January 2016)
- Record Type:
- Journal Article
- Title:
- The orchestra of lipid-transfer proteins at the crossroads between metabolism and signaling. (January 2016)
- Main Title:
- The orchestra of lipid-transfer proteins at the crossroads between metabolism and signaling
- Authors:
- Chiapparino, Antonella
Maeda, Kenji
Turei, Denes
Saez-Rodriguez, Julio
Gavin, Anne-Claude - Abstract:
- Abstract: Within the eukaryotic cell, more than 1000 species of lipids define a series of membranes essential for cell function. Tightly controlled systems of lipid transport underlie the proper spatiotemporal distribution of membrane lipids, the coordination of spatially separated lipid metabolic pathways, and lipid signaling mediated by soluble proteins that may be localized some distance away from membranes. Alongside the well-established vesicular transport of lipids, non-vesicular transport mediated by a group of proteins referred to as lipid-transfer proteins (LTPs) is emerging as a key mechanism of lipid transport in a broad range of biological processes. More than a hundred LTPs exist in humans and these can be divided into at least ten protein families. LTPs are widely distributed in tissues, organelles and membrane contact sites (MCSs), as well as in the extracellular space. They all possess a soluble and globular domain that encapsulates a lipid monomer and they specifically bind and transport a wide range of lipids. Here, we present the most recent discoveries in the functions and physiological roles of LTPs, which have expanded the playground of lipids into the aqueous spaces of cells.
- Is Part Of:
- Progress in lipid research. Volume 61(2016:Jan.)
- Journal:
- Progress in lipid research
- Issue:
- Volume 61(2016:Jan.)
- Issue Display:
- Volume 61 (2016)
- Year:
- 2016
- Volume:
- 61
- Issue Sort Value:
- 2016-0061-0000-0000
- Page Start:
- 30
- Page End:
- 39
- Publication Date:
- 2016-01
- Subjects:
- CERT ceramide transfer protein -- CETP cholesteryl ester transfer protein -- ER endoplasmic reticulum -- FABP fatty acid-binding protein -- FFAT diphenylalanine in an acidic tract -- GAP GTPase-activating protein -- GEF guanine nucleotide exchange factor -- GLs glycerolipids -- GLTP glycolipid transfer protein -- GLTPD1 glycolipid transfer protein domain-containing protein 1 -- GM2A ganglioside GM2 activator protein -- GPL glycerophospholipids -- LTD lipid-transfer domain -- LTP lipid transfer protein -- MCS membrane contact site -- ML MD-2-related lipid-recognition -- NLS nuclear localization sequence -- NPC Niemann–Pick C -- OSBP oxysterol-binding protein -- OSBPL1A oxysterol-binding protein-related protein 1 -- OSBPL9 oxysterol-binding protein-related protein 9 -- PLEKHA8 pleckstrin homology domain-containing family A member 8 -- PPARD peroxisome proliferator-activated receptor δ -- PH pleckstrin homology -- PC phosphatidylcholine -- PI phosphatidylinositol -- PIP phosphatidylinositol phosphate -- PITP PI-transfer protein -- PITPNM1 membrane-associated PITP 1 -- PM plasma membrane -- PS phosphatidylserine -- RARΑ retinoic acid receptor α -- SL sphingolipids -- SCP2 sterol carrier protein 2 -- StAR steroidogenic acute regulatory protein -- START StAR-related lipid-transfer -- TGN trans-Golgi network -- TSPO translocator protein -- VAPA vesicle-associated membrane protein-associated protein A
Signaling lipid -- Biological membranes -- Non-vesicular lipid trafficking -- Metabolism -- Transport -- Lipid-transfer proteins -- Lipid-binding domains -- Membrane contact sites -- Organelles -- Systems biology -- Biomolecular networks
Lipids -- Periodicals
Lipids -- Periodicals
Lipides -- Périodiques
Lipiden
572.57 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01637827 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.plipres.2015.10.004 ↗
- Languages:
- English
- ISSNs:
- 0163-7827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6868.640000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2054.xml