We are analyzing https://link.springer.com/article/10.1007/s00018-012-1247-3.

Title:
Insights into the mechanisms of sterol transport between organelles | Cellular and Molecular Life Sciences
Description:
In cells, the levels of sterol vary greatly among organelles. This uneven distribution depends largely on non-vesicular routes of transfer, which are mediated by soluble carriers called lipid-transfer proteins (LTPs). These proteins have a domain with a hydrophobic cavity that accommodates one sterol molecule. However, a demonstration of their role in sterol transport in cells remains difficult. Numerous LTPs also contain membrane-binding elements, but it is not clear how these LTPs couple their ability to target organelles with lipid transport activity. This issue appears critical, since many sterol transporters are thought to act at contact sites between two membrane-bound compartments. Here, we emphasize that biochemical and structural studies provide precious insights into the mode of action of sterol-binding proteins. Recent studies on START, Osh/ORP and NPC proteins suggest models on how these proteins could transport sterol between organelles and, thereby, influence cellular functions.
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Keywords {🔍}

google, scholar, pubmed, cas, protein, biol, cell, lipid, cholesterol, sterol, transport, binding, membrane, transfer, proteins, yeast, sci, golgi, chem, oxysterolbinding, biophys, usa, trafficking, mol, proc, natl, acad, domain, start, npc, niemannpick, biochim, acta, stard, function, structure, phosphatidylinositol, regulatory, res, membranes, brown, oxysterol, goldstein, article, endoplasmic, reticulum, plasma, intracellular, role, steroidogenic,

Topics {✒️}

sterol-binding protein kes1/osh4p bruno antonny & guillaume drin endosome-trans-golgi trafficking pathways month download article/chapter lipid-dependent protein sorting oxysterol-binding protein homologues oxysterol-binding protein recognises protein-interacting ffat motif sec14p-dependent protein transport 3-hydroxy-3-methylglutaryl-coa reductase myosin-v-dependent transport yeast oxysterol-binding proteins anti-atherogenic lipid phenotype star-related lipid transfer cholesterol-binding protein deficient membrane-trafficking sorting hubs vesicle-mediated protein transport blanchette-mackie ej lipid-regulated sterol transfer methyl-β-cyclodextrin npc niemann–pick c2 essential human monocyte/macrophages induces golgi apparatus requires oxysterol-binding protein oxysterol binding protein osh/orp de matteis ma guillaume drin intracellular sterol-lipid distribution putative sterol-sensing domain issue appears critical npc2-mediated cholesterol transfer kes1p shares homology oxysterol-binding proteins regulates sterol binding protein regulates trafficking phosphatidylinositol 4-kinase iialpha niemann–pick c1 niemann–pick type srebp-2 transport triggered golgi apparatus triggered oxysterol-binding domains cholesterol transfer protein osh4p exchanges sterols closely related homologues lipid-transfer proteins lipid binding proteins niemann–pick c2 osbp-related proteins mitochondrial cholesterol transporter

Questions {❓}

Beh CT, Alfaro G, Duamel G, Sullivan DP, Kersting MC, Dighe S, Kozminski KG, Menon AK (2009) Yeast oxysterol-binding proteins: sterol transporters or regulators of cell polarization?
Prinz WA (2010) Lipid trafficking sans vesicles: where, why, how?

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      headline:Insights into the mechanisms of sterol transport between organelles
      description:In cells, the levels of sterol vary greatly among organelles. This uneven distribution depends largely on non-vesicular routes of transfer, which are mediated by soluble carriers called lipid-transfer proteins (LTPs). These proteins have a domain with a hydrophobic cavity that accommodates one sterol molecule. However, a demonstration of their role in sterol transport in cells remains difficult. Numerous LTPs also contain membrane-binding elements, but it is not clear how these LTPs couple their ability to target organelles with lipid transport activity. This issue appears critical, since many sterol transporters are thought to act at contact sites between two membrane-bound compartments. Here, we emphasize that biochemical and structural studies provide precious insights into the mode of action of sterol-binding proteins. Recent studies on START, Osh/ORP and NPC proteins suggest models on how these proteins could transport sterol between organelles and, thereby, influence cellular functions.
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         Lipid transfer protein
         Osh/ORP
         START
         Cell Biology
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         general
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         Biochemistry
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