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A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport

Gatta, AT; Wong, LH; Sere, YY; Calderón-Noreña, DM; Cockcroft, S; Menon, AK; Levine, TP; (2015) A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport. Elife , 4 , Article e07253. 10.7554/eLife.07253. Green open access

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Abstract

Sterol traffic between the endoplasmic reticulum (ER) and plasma membrane (PM) is a fundamental cellular process that occurs by a poorly understood non-vesicular mechanism. We identified a novel, evolutionarily diverse family of ER membrane proteins with StART-like lipid transfer domains and studied them in yeast. StART-like domains from Ysp2p and its paralog Lam4p specifically bind sterols, and Ysp2p, Lam4p and their homologs Ysp1p and Sip3p target punctate ER-PM contact sites distinct from those occupied by known ER-PM tethers. The activity of Ysp2p, reflected in amphotericin-sensitivity assays, requires its second StART-like domain to be positioned so that it can reach across ER-PM contacts. Absence of Ysp2p, Ysp1p or Sip3p reduces the rate at which exogenously supplied sterols traffic from the PM to the ER. Our data suggest that these StART-like proteins act in trans to mediate a step in sterol exchange between the PM and ER.

Type: Article
Title: A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.7554/eLife.07253
Publisher version: http://dx.doi.org/10.7554/eLife.07253
Language: English
Additional information: This is an Open Access article distributed under the terms of the Creative Commons Attribution 4.0 International (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Keywords: S. cerevisiae, StART protein, VASt domains, cell biology, cholesterol, ergosterol, lipid traffic, membrane contact sites, polyenes
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Neuro, Physiology and Pharmacology
URI: https://discovery.ucl.ac.uk/id/eprint/1473395
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