Evidence map›Paper›PMID 28841344›Full record

ReviewAnnual review of biochemistry2018

Retrospective on Cholesterol Homeostasis: The Central Role of Scap.

Michael S Brown, Arun Radhakrishnan, Joseph L Goldstein

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 294 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
294citing papers in PubMed, 2 pooled it
28.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

294 citing papers in PubMed, 2 syntheses or guidelines pooled it, 471 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  7. Singlet oxygen spills sterol secrets.Nature chemical biology · 2026
    Article
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  9. Review
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  15. Visualization of the interaction between sphingomyelin and cholesterol in lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Review
  17. Article
  18. Article
  19. Review
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234 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Michael S BrownDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA; email: mike.brown@utsouthwestern.edu ; joe.goldstein@utsouthwestern.edu.
Arun RadhakrishnanDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA; email: mike.brown@utsouthwestern.edu ; joe.goldstein@utsouthwestern.edu.
Joseph L GoldsteinDepartment of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA; email: mike.brown@utsouthwestern.edu ; joe.goldstein@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

TRANSCRIPTIONAL REGULATION OF LDL RECEPTOR PROMOTERP01HL020948 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI GOLDSTEIN, JOSEPH L · 1985 to 2021
$103.1M
NHLBI NIH HHS P01 HL020948
6 · The paper itself

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.

Indexed as

AnimalsCholesterolHomeostasisHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsModels, BiologicalModels, MolecularProtein ConformationProtein TransportProteolysisReceptors, LDLSterol Regulatory Element Binding ProteinsCholesterolIntracellular Signaling Peptides and ProteinsMembrane ProteinsReceptors, LDLSREBP cleavage-activating proteinSterol Regulatory Element Binding Proteinscholesterolconformational changesCOPII vesiclesER-to-Golgi transportInsigmembrane proteinsproteolytic processingScapSREBPstranscriptional regulation

Identifiers

PMID28841344
PMCPMC5828883
OpenAlexW2745669578

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.