Evidence map›Paper›PMID 11071899›Full record

ArticleMolecular biology of the cell2000

ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membrane.

C W Joyce, G S Shelness, M A Davis, R G Lee, K Skinner, R A Anderson, L L Rudel

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
7.5field-weighted citation impact, top 3% 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

41 citing papers in PubMed, 114 citations in OpenAlex.

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  10. An overview of ghrelinExpert opinion on therapeutic patents · 2020
    Review
  11. Article
  12. Mechanisms and regulation of cholesterol homeostasis.Nature reviews. Molecular cell biology · 2020
    Review
  13. Article
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  15. Oncotarget · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

7 authors at 1 institution in 1 country.

C W JoyceDepartment of Pathology, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA.
G S Shelness
M A Davis
R G Lee
K Skinner
R A Anderson
L L Rudel
Wake Forest University · US

Funding

TISSUE CULTURE COREP01HL049373 · NHLBI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI SHELNESS, GREGORY S · 1993 to 2012
$23.8M
CARDIOVASCULAR PATHOLOGYT32HL007115 · NHLBI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI ST CLAIR, RICHARD W · 1985 to 2004
$1.6M
NHLBI NIH HHS HL-07115NHLBI NIH HHS HL-49373NHLBI NIH HHS P01 HL049373NHLBI NIH HHS T32 HL007115
6 · The paper itself

Abstract

A second form of the enzyme acyl-CoA:cholesterol acyltransferase, ACAT2, has been identified. To explore the hypothesis that the two ACAT enzymes have separate functions, the membrane topologies of ACAT1 and ACAT2 were examined. A glycosylation reporter and FLAG epitope tag sequence was appended to a series of ACAT cDNAs truncated after each predicted transmembrane domain. Fusion constructs were assembled into microsomal membranes, in vitro, and topologies were determined based on glycosylation site use and accessibility to exogenous protease. The accessibility of the C-terminal FLAG epitope in constructs was determined by immunofluorescence microscopy of permeabilized transfected cells. Both ACAT1 and ACAT2 span the membrane five times with their N termini in the cytosol and C termini in the ER lumen. The fourth transmembrane domain is located in a different region for each protein, placing the putative active site ACAT1 serine (Ser(269)) in the cytosol and the analogous residue in ACAT2 (Ser(249)) in the ER lumen. Mutation of these serines inactivated the ACAT enzymes. The outcome is consistent with the hypothesis that cholesterol ester formation by ACAT2 may be coupled to lipoprotein particle assembly and secretion, whereas ACAT1 may function primarily to maintain the balance of free and esterified cholesterol intracellularly.

Indexed as

SerineAnimalsCHO CellsComputer SimulationCricetinaeEndoplasmic ReticulumIntracellular MembranesIsoenzymesModels, MolecularMutagenesis, Site-DirectedRecombinant Fusion ProteinsSterol O-AcyltransferaseIsoenzymesRecombinant Fusion ProteinsSerineSterol O-Acyltransferase

Identifiers

PMID11071899
PMCPMC15029
OpenAlexW2167670101

What OpenQuestion holds

Textmetadata
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.