Evidence map›Paper›PMID 28992438›Full record

ReviewAnnual review of cell and developmental biology2017

Proteostatic Tactics in the Strategy of Sterol Regulation.

Margaret A Wangeline, Nidhi Vashistha, Randolph Y Hampton

Abstract readReview
In one paragraph

Review in Annual review of cell and developmental biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Post-Translational Regulation of HMG CoA Reductase.Cold Spring Harbor perspectives in biology · 2022
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Margaret A WangelineSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, California 92093; email: rhampton@ucsd.edu.
Nidhi VashisthaSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, California 92093; email: rhampton@ucsd.edu.
Randolph Y HamptonSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, California 92093; email: rhampton@ucsd.edu.

Funding

GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
Protein degradation and cholesterol regulationR37DK051996 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 2012 to 2020
$3.2M
NIDDK NIH HHS R37 DK051996NIGMS NIH HHS T32 GM007240
6 · The paper itself

Abstract

In eukaryotes, the synthesis and uptake of sterols undergo stringent multivalent regulation. Both individual enzymes and transcriptional networks are controlled to meet changing needs of the many sterol pathway products. Regulation is tailored by evolution to match regulatory constraints, which can be very different in distinct species. Nevertheless, a broadly conserved feature of many aspects of sterol regulation is employment of proteostasis mechanisms to bring about control of individual proteins. Proteostasis is the set of processes that maintain homeostasis of a dynamic proteome. Proteostasis includes protein quality control pathways for the detection, and then the correction or destruction, of the many misfolded proteins that arise as an unavoidable feature of protein-based life. Protein quality control displays not only the remarkable breadth needed to manage the wide variety of client molecules, but also extreme specificity toward the misfolded variants of a given protein. These features are amenable to evolutionary usurpation as a means to regulate proteins, and this approach has been used in sterol regulation. We describe both well-trod and less familiar versions of the interface between proteostasis and sterol regulation and suggest some underlying ideas with broad biological and clinical applicability.

Indexed as

ProteostasisAnimalsEndoplasmic Reticulum-Associated DegradationHumansLipid MetabolismSignal TransductionSterol Regulatory Element Binding ProteinsSterolsSterol Regulatory Element Binding ProteinsSterolsERADHMG-CoA reductaseHrd1INSIGSCAPSSD

Identifiers

PMID28992438
PMCPMC6037418

What OpenQuestion holds

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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.