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

Gatta, Alberto T, Wong, Louise H, Sere, Yves Y, Calderón-Noreña, Diana M, Cockcroft, Shamshad, Menon, Anant K, Levine, Tim P·2015·eLife
DOI 10.7554/elife.07253PMC PMC4463742
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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.

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  • GRAMD1 proteins (GRAMD1a/1b/1c) mediate non-vesicular transport of accessible cholesterol from the plasma membrane to the endoplasmic reticulum at ER-PM contact sites, contributing to cholesterol homeostasis.

    “Transport of the “accessible” pool of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) by ER‐localized GRAMD1 proteins (GRAMD1a/1b/1c) contributes to cholesterol homeostasis.”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Gatta et al, 2015

    The Results section on sterol transport reports that yeast Ysp1p, Ysp2p and Sip3p appear to act in non-vesicular PM-to-ER sterol transport. The Discussion identifies GramD1a–c as related human proteins but says little is known about them. The paper therefore does not establish that GRAMD1a/1b/1c transport the accessible cholesterol pool or contribute to cholesterol homeostasis. (LLM, conf=0.90)

    Experimental — accuracy not yet measured

  • Yeast mutants that lack GRAMD1 homologs (Lam/Ltc proteins) are highly susceptible to treatment with the polyene antibiotic Amphotericin B compared to WT cells.

    “Yeast mutants that lack GRAMD1 homologs (Lam/Ltc proteins) are highly susceptible to treatment with the polyene antibiotic, Amphotericin B, compared to WT cells (Gatta et al, 2015; Marek et al, 2020).”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Gatta et al, 2015

    The Results section (‘Ysp2p function correlates with sterol binding to its StART-like domain’; Figure 4A) reports that Δysp1 and Δsip3 were highly sensitive to amphotericin B compared with wild type. But Δysp2 was only moderately sensitive, while Δlam4, Δlam5 and Δlam6 behaved like wild type, so the claim is too broad for mutants lacking Lam/Ltc proteins generally. (LLM, conf=0.91)

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Metadata

Authors
Gatta, A. T., Wong, L. H., Sere, Y. Y., Calderón-Noreña, D. M., Cockcroft, S., Menon, A. K., & Levine, T. P.
Venue
eLife
Publisher
eLife Sciences Publications, Ltd
Published
2015-05-22
Volume
4
ISSN
2050-084X
DOI
10.7554/elife.07253
PMC
PMC4463742
Cited by
251
References
6
Language
en
Licence
Funders
  • Qatar National Research Fund (QNRF) (NPRP 5-669-1-112)
  • Medical Research Council (MRC) (MR/J006580/1)
  • European Commission (Sphingonet ITN, project ref 289278)

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