Evidence map›Paper›PMID 26621918›Full record

ArticleJournal of lipid research2016

Association of NMT2 with the acyl-CoA carrier ACBD6 protects the N-myristoyltransferase reaction from palmitoyl-CoA.

Eric Soupene, Joseph Kao, Daniel H Cheng, Derek Wang, Alexander L Greninger, Giselle M Knudsen, Joseph L DeRisi, Frans A Kuypers

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Amino acid and protein specificity of protein fatty acylation inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Acylation - A New Means to Control Traffic Through the Golgi.Frontiers in cell and developmental biology · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Review
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

8 authors at 2 institutions in 1 country.

Eric SoupeneChildren's Hospital Oakland Research Institute, Oakland, CA esoupene@chori.org.
Joseph KaoChildren's Hospital Oakland Research Institute, Oakland, CA.
Daniel H ChengChildren's Hospital Oakland Research Institute, Oakland, CA.
Derek WangChildren's Hospital Oakland Research Institute, Oakland, CA.
Alexander L GreningerDepartment of Biochemistry and Biophysics, University of California at San Francisco and Howard Hughes Medical Institute, San Francisco, CA.
Giselle M KnudsenDepartment of Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, CA.
Joseph L DeRisiDepartment of Biochemistry and Biophysics, University of California at San Francisco and Howard Hughes Medical Institute, San Francisco, CA.
Frans A KuypersChildren's Hospital Oakland Research Institute, Oakland, CA.
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007618 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ANDERSON, MARK S · 1985 to 2020
$29.6M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Howard Hughes Medical InstituteNIGMS NIH HHS 8P41GM103481NIGMS NIH HHS P41 GM103481NIGMS NIH HHS T32 GM007618
6 · The paper itself

Abstract

The covalent attachment of a 14-carbon aliphatic tail on a glycine residue of nascent translated peptide chains is catalyzed in human cells by two N-myristoyltransferase (NMT) enzymes using the rare myristoyl-CoA (C(14)-CoA) molecule as fatty acid donor. Although, NMT enzymes can only transfer a myristate group, they lack specificity for C(14)-CoA and can also bind the far more abundant palmitoyl-CoA (C(16)-CoA) molecule. We determined that the acyl-CoA binding protein, acyl-CoA binding domain (ACBD)6, stimulated the NMT reaction of NMT2. This stimulatory effect required interaction between ACBD6 and NMT2, and was enhanced by binding of ACBD6 to its ligand, C(18:2)-CoA. ACBD6 also interacted with the second human NMT enzyme, NMT1. The presence of ACBD6 prevented competition of the NMT reaction by C(16)-CoA. Mutants of ACBD6 that were either deficient in ligand binding to the N-terminal ACBD or unable to interact with NMT2 did not stimulate activity of NMT2, nor could they protect the enzyme from utilizing the competitor C(16)-CoA. These results indicate that ACBD6 can locally sequester C(16)-CoA and prevent its access to the enzyme binding site via interaction with NMT2. Thus, the ligand binding properties of the NMT/ACBD6 complex can explain how the NMT reaction can proceed in the presence of the very abundant competitive substrate, C(16)-CoA.

Indexed as

AcylationAcyl Coenzyme AAcyltransferasesATP-Binding Cassette TransportersCarrier ProteinsCoenzyme AFatty AcidsHumansMembrane LipidsMyristic AcidPalmitoyl Coenzyme APhospholipidsProtein Interaction Domains and MotifsSubstrate SpecificityACBD6 protein, humanAcyl Coenzyme AAcyltransferasesATP-Binding Cassette TransportersCarrier ProteinsCoenzyme AFatty Acidsglycylpeptide N-tetradecanoyltransferaseMembrane LipidsMyristic AcidPalmitoyl Coenzyme APhospholipidsS-tetradecanoyl-coenzyme Abinding proteincoenzyme AmembranesN-myristoyltransferase 2phospholipidsprotein acylationprotein interaction

Identifiers

PMID26621918
PMCPMC4727424
OpenAlexW2256421302

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.