Evidence map›Paper›PMID 16834775›Full record

ArticleBMC molecular biology2006

Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains.

Eric Soupene, Frans A Kuypers

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. The impact of lipid metabolism on ferroptosis in myocardial ischemia-reperfusion injury.Apoptosis : an international journal on programmed cell death · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
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  11. Acyl-CoA synthetases as regulators of brain phospholipid acyl-chain diversity.Prostaglandins, leukotrienes, and essential fatty acids · 2020
    Review
  12. Article
  13. A novel transgenic mouse model of lysosomal storage disorder.American journal of physiology. Gastrointestinal and liver physiology · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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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

2 authors at 1 institution in 1 country.

Eric SoupeneChildren's Hospital Oakland Research Institute, Oakland, California 94609, USA. esoupene@chori.org
Frans A Kuypers
Environmental Systems Research Institute (United States) · US

Funding

SICKLE CELL SCHOLAR PLANU54HL070583 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI VICHINKSY, ELLIOTT P. · 2003 to 2010
$12.0M
NHLBI NIH HHS HL070583NHLBI NIH HHS U54 HL070583
6 · The paper itself

Abstract

backgroundThe formation of acyl-CoA by the action of acyl-CoA synthetases plays a crucial role in membrane lipid turnover, including the plasma membrane of erythrocytes. In human, five Acyl-CoA Synthetase Long-chain (ACSL) genes have been identified with as many as 3 different transcript variants for each.

resultsAcyl-CoA Synthetase Long-chain member 6 (ACSL6) is responsible for activation of long-chain fatty acids in erythrocytes. Two additional transcript variants were also isolated from brain and testis. We report the expression in reticulocytes of two new variants and of the one isolated from brain. All three represented different spliced variants of a mutually exclusive exon pair. They encode a slightly different short motif which contains a conserved structural domain, the fatty acid Gate domain. The motifs differ in the presence of either the aromatic residue phenylalanine (Phe) or tyrosine (Tyr). Based on homology, two new isoforms for the closely related ACSL1 were predicted and characterized. One represented a switch of the Phe- to the Tyr-Gate domain motif, the other resulted from the exclusion of both. Swapping of this motif also appears to be common in all mammalian ACSL member 1 and 6 homologs.

conclusionWe propose that a Phe to Tyr substitution or deletion of the Gate domain, is the structural reason for the conserved alternative splicing that affects these motifs. Our findings support our hypothesis that this region is structurally important to define the activity of these enzymes.

Indexed as

Alternative SplicingAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCell MembraneCoenzyme A LigasesConserved SequenceExonsFatty AcidsHumansIsoenzymesLong-Chain-Fatty-Acid-CoA LigaseMiceMolecular Sequence DataPan troglodytesACSL6 protein, humanCoenzyme A LigasesFatty AcidsIsoenzymesLong-Chain-Fatty-Acid-CoA Ligase

Identifiers

PMID16834775
PMCPMC1543647
OpenAlexW1827831627

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.