Evidence map›Paper›PMID 30393067›Full record

ArticleCell chemical biology2019

Synthetic Fluorogenic Peptides Reveal Dynamic Substrate Specificity of Depalmitoylases.

Neri Amara, Ian T Foe, Ouma Onguka, Megan Garland, Matthew Bogyo

Abstract read
In one paragraph

Article in Cell chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  3. Depalmitoylation and cell physiology: APT1 as a mediator of metabolic signals.American journal of physiology. Cell physiology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Pathogens (Basel, Switzerland) · 2022
    Article
  9. Glycosylation Analysis of Feline Small Intestine FollowingAnimals : an open access journal from MDPI · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Upregulation of Cellular Palmitoylation Mitigates α-Synuclein Accumulation and Neurotoxicity.Movement disorders : official journal of the Movement Disorder Society · 2021
    Article
  14. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  15. Article
  16. Article
  17. Activity-Based Sensing ofAccounts of chemical research · 2019
    Review
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Neri AmaraDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Ian T FoeDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Ouma OngukaDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Megan GarlandDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Matthew BogyoDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: mbogyo@stanford.edu.

Funding

Equipment supplement for Chemical methods to study protein palmitoylation pathwaysR01GM111703 · NIGMS · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2014 to 2017
$1.6M
NIGMS NIH HHS R01 GM111703
6 · The paper itself

Abstract

Palmitoylation is a post-translational modification involving the thioesterification of cysteine residues with a 16-carbon-saturated fatty acid. Little is known about rates of depalmitoylation or the parameters that dictate these rates. Here we report a modular strategy to synthesize quenched fluorogenic substrates for the specific detection of depalmitoylase activity and for mapping the substrate specificity of individual depalmitoylases. We demonstrate that human depalmitoylases APT1 and APT2, and TgPPT1 from the parasite Toxoplasma gondii, have distinct specificities that depend on amino acid residues distal to the palmitoyl cysteine. This information informs the design of optimal and non-optimal substrates as well as isoform-selective substrates to detect the activity of a specific depalmitoylase in complex proteomes. In addition to providing tools for studying depalmitoylases, our findings identify a previously unrecognized mechanism for regulating steady-state levels of distinct palmitoylation sites by sequence-dependent control of depalmitoylation rates.

Indexed as

AnimalsCell LineFemaleFluorescent DyesHumansMembrane ProteinsMiceMice, Inbred C57BLMolecular StructurePeptidesSubstrate SpecificityThiolester HydrolasesToxoplasmaFluorescent DyesLYPLA1 protein, humanLYPLA2 protein, humanMembrane ProteinsPeptidesPPT1 protein, humanThiolester Hydrolaseschemical probescombinatorial librariesdepalmitoylasesdynamic palmitoylationfluorogenic peptidessubstrate specificitythioesterases

Identifiers

PMID30393067
PMCPMC6338520

What OpenQuestion holds

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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.