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Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER

Espenshade, Peter J., Li, Wei-Ping, Yabe, Daisuke·2002·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.182412799
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Abstract

Sterols inhibit their own synthesis in mammalian cells by blocking the vesicular endoplasmic reticulum-to-Golgi transport of sterol regulatory element-binding protein (SREBP) cleavage-activating protein (SCAP), a sterol-sensing protein that escorts SREBPs. Unable to reach the Golgi, SREBPs are not processed by Golgi-resident proteases, and they fail to activate genes required for cholesterol synthesis. The current studies were designed to reveal whether sterols block SCAP movement by inhibiting synthesis of special vesicles dedicated to SCAP, or whether sterols block SCAP incorporation into common coat protein (COP)II-coated vesicles. Through immunoisolation, we show that SCAP-containing vesicles, formed in vitro , also contain vesicular stomatitis virus glycoprotein (VSVG) protein, a classic marker of COPII-coated vesicles. Sterols selectively block incorporation of SCAP into these vesicles without blocking incorporation of VSVG protein. We show that the mammalian vesicular budding reaction can be reconstituted by recombinant yeast COPII proteins that support incorporation of SCAP as well as VSVG into vesicles. Sterols block SCAP incorporation into vesicles by blocking Sar1-dependent binding of the COPII proteins Sec 23/24 to SCAP. These studies demonstrate feedback control of a biosynthetic pathway by the regulated binding of COPII proteins to an endoplasmic reticulum-to-Golgi transport protein.

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Crossref · 10.1073/pnas.182412799

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  • SCAP and SREBP-2 are incorporated into COPII vesicles that bud off the ER and can be transported to the Golgi apparatus.

    “SCAP and SREBP-2 are then incorporated into these COPII vesicles that bud off of the ER and can be transported to the Golgi apparaturs70.”

    From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [70]

  • A drop in ER cholesterol leads to a conformational change in SCAP, dissociation from INSIG, and COPII-mediated trafficking of the SCAP-SREBP complex to the Golgi.

    “A drop in cholesterol in the ER membrane leads to a conformational change in SCAP11,12, which leads to dissociation from INSIG and facilitates COPII-mediated trafficking of the SCAP-SREBP complex to the Golgi13–15.”

    From Haploid genetic screens identify SPRING/C12ORF49 as a determinant of SREBP signaling and cholesterol metabolism (2020) · cites this paper as [15]

  • A decrease in ER-membrane cholesterol content results in dissociation of INSIG from SCAP and COPII-dependent anterograde transport of the SCAP/SREBP complex to the Golgi.

    “A decrease in ER-membrane cholesterol content results in the dissociation of INSIG from SCAP, and COPII-dependent anterograde transport of the SCAP/SREBP complex to the Golgi4,5”

    From Hepatic SREBP signaling requires SPRING to govern systemic lipid metabolism in mice and humans (2023) · cites this paper as [5]

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Metadata

Authors
Espenshade, P. J., Li, W.-P., & Yabe, D.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2002-08-22
Volume
99
Issue
18
Pages
11694-11699
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.182412799
Cited by
133
References
0
Language
en

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