NATURE . COM {
}
We are analyzing https://www.nature.com/articles/s41580-018-0071-5.
Title:
Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes | Nature Reviews Molecular Cell Biology
Description:
Lipids are distributed in a highly heterogeneous fashion in different cellular membranes. Only a minority of lipids achieve their final intracellular distribution through transport by vesicles. Instead, the bulk of lipid traffic is mediated by a large group of lipid transfer proteins (LTPs), which move small numbers of lipids at a time using hydrophobic cavities that stabilize lipid molecules outside membranes. Although the first LTPs were discovered almost 50 years ago, most progress in understanding these proteins has been made in the past few years, leading to considerable temporal and spatial refinement of our understanding of the function of these lipid transporters. The number of known LTPs has increased, with exciting discoveries of their multimeric assembly. Structural studies of LTPs have progressed from static crystal structures to dynamic structural approaches that show how conformational changes contribute to lipid handling at a sub-millisecond timescale. A major development has been the finding that many intracellular LTPs localize to two organelles at the same time, forming a shuttle, bridge or tube that links donor and acceptor compartments. The understanding of how different lipids achieve their final destination at the molecular level allows a better explanation of the range of defects that occur in diseases associated with lipid transport and distribution, opening up the possibility of developing therapies that specifically target lipid transfer. The distribution of lipids largely depends on their non-vesicular transport by lipid transfer proteins (LTPs). Recent progress in understanding the mechanisms of LTPs, including the appreciation of their widespread activity at membrane contact sites, has provided novel insights into the regulation of lipid trafficking and how it impacts pathophysiology.
Website Age:
30 years and 10 months (reg. 1994-08-11).
Title:
Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes | Nature Reviews Molecular Cell Biology
Description:
Lipids are distributed in a highly heterogeneous fashion in different cellular membranes. Only a minority of lipids achieve their final intracellular distribution through transport by vesicles. Instead, the bulk of lipid traffic is mediated by a large group of lipid transfer proteins (LTPs), which move small numbers of lipids at a time using hydrophobic cavities that stabilize lipid molecules outside membranes. Although the first LTPs were discovered almost 50 years ago, most progress in understanding these proteins has been made in the past few years, leading to considerable temporal and spatial refinement of our understanding of the function of these lipid transporters. The number of known LTPs has increased, with exciting discoveries of their multimeric assembly. Structural studies of LTPs have progressed from static crystal structures to dynamic structural approaches that show how conformational changes contribute to lipid handling at a sub-millisecond timescale. A major development has been the finding that many intracellular LTPs localize to two organelles at the same time, forming a shuttle, bridge or tube that links donor and acceptor compartments. The understanding of how different lipids achieve their final destination at the molecular level allows a better explanation of the range of defects that occur in diseases associated with lipid transport and distribution, opening up the possibility of developing therapies that specifically target lipid transfer. The distribution of lipids largely depends on their non-vesicular transport by lipid transfer proteins (LTPs). Recent progress in understanding the mechanisms of LTPs, including the appreciation of their widespread activity at membrane contact sites, has provided novel insights into the regulation of lipid trafficking and how it impacts pathophysiology.
Website Age:
30 years and 10 months (reg. 1994-08-11).
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Keywords {🔍}
pubmed, article, google, scholar, cas, central, lipid, membrane, transfer, cell, protein, biol, proteins, nature, transport, cholesterol, structural, contact, sites, mol, chem, sterol, structure, lipids, phosphatidylinositol, yeast, sci, binding, nat, membranes, ltps, access, plasma, domain, domains, exchange, content, molecular, levine, crystal, basis, homeostasis, proc, natl, acad, usa, phospholipid, analysis, studies, mechanism,
Topics {✒️}
nature portfolio journals permissions reprints medical research council nature portfolio privacy policy cytosolic megakaryocyte protein-tyrosine-phosphatase advertising control rab7-rilp-p150 glued resistance-nodulation-division efflux transporters major development social media niemann–pick c1 protein cral-trio protein family niemann-pick c2 essential er-mitochondria contact sites phosphatidic acid-binding protein cholesterol-regulated scaffolding protein fatty acid-binding protein nature+ nature 510 nature 391 nature 501 nature 426 nature strong pro-inflammatory molecule er-pm sterol transport sec14p-dependent protein transport cellular retinaldehyde-binding protein widespread dual-membrane targeting studies cement counter-current er-localized sterol transporter lipid-bound extended synaptotagmin personal data gram-negative outer membrane phosphatidylinositol–phosphatidic acid exchange bpi–cetp–pltp family author correspondence lipid counter-current mechanism er–mitochondrial encounter structure er–golgi tether osbp hydrolysis directs sterol/pi data protection permissions secreted sterol-binding proteins springerlink instant access article presents extensive newly synthesized sterol oxysterol binding protein mdm12/mmm1 ermes complexes er-vacuole contacts
Questions {❓}
- Function of the phosphatidylinositol transfer protein gene family: is phosphatidylinositol transfer the mechanism of action?
- Is ABCA1 a lipid transfer protein?
- Lipid transfer proteins do their thing anchored at membrane contact sites… but what is their thing?
- PIP3, PIP2, and cell movement — similar messages, different meanings?
Schema {🗺️}
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