Evidence map›Paper›PMID 31969037›Full record

ReviewMolecular membrane biology2019

Spatial organization of palmitoyl acyl transferases governs substrate localization and function.

Julie M Philippe, Paul M Jenkins

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular membrane biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Altered Protein Palmitoylation as Disease Mechanism in Neurodegenerative Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Ankyrin-B is lipid-modified byFrontiers in physiology · 2023
    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

2 authors at 1 institution in 1 country.

Julie M PhilippeDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, USA.ORCID 0000-0002-3517-4284
Paul M JenkinsDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, MI, USA.ORCID 0000-0002-4207-5823
University of Michigan · US

Funding

INTERDEPARTMENTAL TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007767 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ISOM, LORI L. · 1985 to 2019
$10.2M
NIGMS NIH HHS T32 GM007767
6 · The paper itself

Abstract

Protein palmitoylation is a critical posttranslational modification that regulates protein trafficking, localization, stability, sorting and function. In mammals, addition of this lipid modification onto proteins is mediated by a family of 23 palmitoyl acyl transferases (PATs). PATs often palmitoylate substrates in a promiscuous manner, precluding our understanding of how these enzymes achieve specificity for their substrates. Despite generous efforts to identify consensus motifs defining PAT-substrate specificity, it remains to be determined whether additional factors beyond interaction motifs, such as local palmitoylation, participate in PAT-substrate selection. In this review, we emphasize the role of local palmitoylation, in which substrates are palmitoylated and trapped in the same subcellular compartments as their PATs, as a mechanism of enzyme-substrate specificity. We focus here on non-Golgi-localized PATs, as physical proximity to their substrates enables them to engage in local palmitoylation, compared to Golgi PATs, which often direct trafficking of their substrates elsewhere. PAT subcellular localization may be an under-recognized, yet important determinant of PAT-substrate specificity that may work in conjunction or completely independently of interaction motifs. We also discuss some current hypotheses about protein motifs that contribute to localization of non-Golgi-localized PATs, important for the downstream targeting of their substrates.

Indexed as

LipoylationProtein Processing, Post-TranslationalAcyltransferasesAnimalsHumansMembrane ProteinsProtein TransportSubstrate SpecificityAcyltransferasesMembrane Proteinslipidlocalizationmembrane microdomainsPalmitoylationpolaritytraffickingzDHHC enzymes

Identifiers

PMID31969037
PMCPMC7031816
OpenAlexW3001143557

What OpenQuestion holds

Textmetadata
LicenceTDM
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.