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Retrospective on Cholesterol Homeostasis: The Central Role of Scap

Brown, Michael S., Radhakrishnan, Arun, Goldstein, Joseph L.·2018·Annual Review of Biochemistry
DOI 10.1146/annurev-biochem-062917-011852PMC PMC5828883
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Abstract

Scap is a polytopic membrane protein that functions as a molecular machine to control the cholesterol content of membranes in mammalian cells. In the 21 years since our laboratory discovered Scap, we have learned how it binds sterol regulatory element-binding proteins (SREBPs) and transports them from the endoplasmic reticulum (ER) to the Golgi for proteolytic processing. Proteolysis releases the SREBP transcription factor domains, which enter the nucleus to promote cholesterol synthesis and uptake. When cholesterol in ER membranes exceeds a threshold, the sterol binds to Scap, triggering several conformational changes that prevent the Scap–SREBP complex from leaving the ER. As a result, SREBPs are no longer processed, cholesterol synthesis and uptake are repressed, and cholesterol homeostasis is restored. This review focuses on the four domains of Scap that undergo concerted conformational changes in response to cholesterol binding. The data provide a molecular mechanism for the control of lipids in cell membranes.

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  • Association of SREBPs with SCAP and INSIG couples their ER retention and proteolytic activation to sensing of ER membrane cholesterol by SCAP.

    “Their association in a complex with SCAP and INSIG couples their retention in the ER and subsequent proteolytic activation to the sensing of cholesterol content in the ER membrane by SCAP1–3.”

    From Hepatic SREBP signaling requires SPRING to govern systemic lipid metabolism in mice and humans (2023) · cites this paper as [3]

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Metadata

Authors
Brown, M. S., Radhakrishnan, A., & Goldstein, J. L.
Affiliations
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA;
Venue
Annual Review of Biochemistry
Publisher
Annual Reviews
Published
2018-06-20
Volume
87
Issue
1
Pages
783-807
ISSN
  • 0066-4154
  • 1545-4509
DOI
10.1146/annurev-biochem-062917-011852
PMC
PMC5828883
Cited by
477
References
2
Language
en
Licence
www.annualreviews.org/licenses/tdm (tdm)

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