دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.
المؤلفون: Gatta AT; Department of Cell Biology, UCL Institute of Ophthalmology, London, United Kingdom., Wong LH; Department of Cell Biology, UCL Institute of Ophthalmology, London, United Kingdom., Sere YY; Department of Biochemistry, Weill Cornell Medical College, New York, United States., Calderón-Noreña DM; Department of Biochemistry, Weill Cornell Medical College, New York, United States., Cockcroft S; Department of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom., Menon AK; Department of Biochemistry, Weill Cornell Medical College, New York, United States., Levine TP; Department of Cell Biology, UCL Institute of Ophthalmology, London, United Kingdom.
المصدر: ELife [Elife] 2015 May 22; Vol. 4. Date of Electronic Publication: 2015 May 22.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Carrier Proteins/*metabolism , Cell Membrane/*metabolism , Endoplasmic Reticulum/*metabolism , Mitochondrial Proteins/*metabolism , Saccharomyces cerevisiae Proteins/*metabolism , Sterols/*metabolism, Biological Transport/physiology ; Computational Biology ; HL-60 Cells ; Humans ; Plasmids/genetics ; Polymerase Chain Reaction
مستخلص: 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.
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معلومات مُعتمدة: BB/M011801/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; MR/J006580/1 United Kingdom MRC_ Medical Research Council
فهرسة مساهمة: Keywords: S. cerevisiae; StART protein; VASt domains; cell biology; cholesterol; ergosterol; lipid traffic; membrane contact sites; polyenes
المشرفين على المادة: 0 (Carrier Proteins)
0 (Mitochondrial Proteins)
0 (Saccharomyces cerevisiae Proteins)
0 (Sterols)
0 (Ysp2 protein, S cerevisiae)
تواريخ الأحداث: Date Created: 20150523 Date Completed: 20160308 Latest Revision: 20210109
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC4463742
DOI: 10.7554/eLife.07253
PMID: 26001273
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.07253