Evidence map›Paper›PMID 24811172›Full record

ArticleThe Journal of biological chemistry2014

Mutations in the X-linked intellectual disability gene, zDHHC9, alter autopalmitoylation activity by distinct mechanisms.

David A Mitchell, Laura D Hamel, Krishna D Reddy, Lynn Farh, Logan M Rettew, Phillip R Sanchez, Robert J Deschenes

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Insights into auto-RSC chemical biology · 2021
    Review
  14. Review
  15. Mutation inNeurology. Genetics · 2021
    Article
  16. Review
  17. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  18. Article
  19. Review
  20. 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

7 authors.

David A MitchellFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and.
Laura D HamelFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and.
Krishna D ReddyFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and.
Lynn Farhthe Department of Chemical Biology, National Pingtung University, Pingtung 900-03, Taiwan.
Logan M RettewFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and.
Phillip R SanchezFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and.
Robert J DeschenesFrom the Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612 and rdeschen@health.usf.edu.

Funding

STRUCTURAL CHANGES AND THE FUNCTION OF RAS ONCOGENESR01CA050211 · NCI · UNIVERSITY OF SOUTH FLORIDA · PI DESCHENES, ROBERT J · 1990 to 2010
$2.2M
Endomembrane Targeting and Signaling of RAS ProteinsR01GM073977 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI DESCHENES, ROBERT J · 2008 to 2011
$1.1M
Protein Palmitoylation and the Etiology of X-Linked Intellectual DisabilitiesR21NS090160 · NINDS · UNIVERSITY OF SOUTH FLORIDA · PI DESCHENES, ROBERT J · 2016 to 2017
$411k
NCI NIH HHS CA050211NCI NIH HHS R01 CA050211NIGMS NIH HHS GM073977NIGMS NIH HHS R01 GM073977NINDS NIH HHS R21 NS090160
6 · The paper itself

Abstract

Early onset intellectual disabilities result in significant societal and economic costs and affect 1-3% of the population. The underlying genetic determinants are beginning to emerge and are interpreted in the context of years of work characterizing postsynaptic receptor and signaling functions of learning and memory. DNA sequence analysis of intellectual disability patients has revealed greater than 80 loci on the X-chromosome that are potentially linked to disease. One of the loci is zDHHC9, a gene encoding a Ras protein acyltransferase. Protein palmitoylation is a reversible modification that controls the subcellular localization and distribution of membrane receptors, scaffolds, and signaling proteins required for neuronal plasticity. Palmitoylation occurs in two steps. In the first step, autopalmitoylation, an enzyme-palmitoyl intermediate is formed. During the second step, the palmitoyl moiety is transferred to a protein substrate, or if no substrate is available, hydrolysis of the thioester linkage produces the enzyme and free palmitate. In this study, we demonstrate that two naturally occurring variants of zDHHC9, encoding R148W and P150S, affect the autopalmitoylation step of the reaction by lowering the steady state amount of the palmitoyl-zDHHC9 intermediate.

Indexed as

Mutation, MissenseAcyltransferasesAmino Acid SequenceChromosomes, Human, XFemaleHumansIntellectual DisabilityLipoylationMaleMolecular Sequence DataAcyltransferasesZDHHC9 protein, humanEnzyme MechanismPost-translational Modification (PTM)Protein AcylationProtein PalmitoylationRas ProteinX-linked Intellectual DisabilityzDHHC Proteins

Identifiers

PMID24811172
PMCPMC4140262

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.