Evidence map›Paper›PMID 29023093›Full record

ArticleBiochemistry2018

A Fluorescent Probe with Improved Water Solubility Permits the Analysis of Protein S-Depalmitoylation Activity in Live Cells.

Tian Qiu, Rahul S Kathayat, Yang Cao, Michael W Beck, Bryan C Dickinson

Abstract read
In one paragraph

Article in Biochemistry, 2018. 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
1.3field-weighted citation impact, top 18% 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, 27 citations in OpenAlex.

  1. Recent Overview of Protein Palmitoylation and Profiling Methodologies.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  2. 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. Article
  7. Article
  8. Inhibitors of DHHC family proteins.Current opinion in chemical biology · 2021
    Review
  9. Article
  10. Quantitative Imaging of BiochemistryACS central science · 2020
    Review
  11. Article
  12. Activity-Based Sensing ofAccounts of chemical research · 2019
    Review
  13. Article
  14. Review
  15. Article
  16. 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

5 authors at 1 institution in 1 country.

Tian QiuDepartment of Chemistry, The University of Chicago , Chicago, Illinois 60637, United States.
Rahul S KathayatDepartment of Chemistry, The University of Chicago , Chicago, Illinois 60637, United States.
Yang CaoDepartment of Chemistry, The University of Chicago , Chicago, Illinois 60637, United States.
Michael W BeckDepartment of Chemistry, The University of Chicago , Chicago, Illinois 60637, United States.ORCID 0000-0002-1737-0951
Bryan C DickinsonDepartment of Chemistry, The University of Chicago , Chicago, Illinois 60637, United States.ORCID 0000-0002-9616-1911
University of Chicago · US

Funding

Rapid selection approaches to understand and reprogram proteins and peptidesR35GM119840 · NIGMS · UNIVERSITY OF CHICAGO · PI Bryan Dickinson · 2016 to 2026
$4.8M
NIGMS NIH HHS R35 GM119840
6 · The paper itself

Abstract

S-Palmitoylation is an abundant lipid post-translational modification that is dynamically installed on and removed from target proteins to regulate their activity and cellular localization. A dearth of tools for studying the activities and regulation of protein S-depalmitoylases, thioesterase "erasers" of protein cysteine S-palmitoylation, has contributed to an incomplete understanding of the role of dynamic S-palmitoylation in regulating proteome lipidation. Recently, we developed "depalmitoylation probes" (DPPs), small molecule probes that become fluorescent upon S-depalmitoylase enzymatic activity. To be suitable for application in live cells, the first-generation DPPs relied on a shorter lipid substrate (C8 vs naturally occurring C16), which enhanced solubility and cell permeability. However, the use of an unnatural lipid substrate on the probes potentially limits the utility of the approach. Herein, we present a new member of the DPP family, DPP-5, which features an anionic carboxylate functional group that increases the probe water solubility. The enhanced water solubility of DPP-5 permits the use of a natural, palmitoylated substrate (C16), rather than a surrogate lipid. We show that DPP-5 is capable of monitoring endogenous S-depalmitoylases in live mammalian cells and that it can reveal changes in S-depalmitoylation levels due to lipid stress. DPP-5 should prove to be a useful new tool for probing the regulation of proteome lipidation through dynamic S-depalmitoylation.

Indexed as

Protein Processing, Post-TranslationalActivation, MetabolicAnimalsCarbamatesCysteineFluorescent DyesHEK293 CellsHumansIntravital MicroscopyLipoylationMammalsMicroscopy, FluorescencePalmitatesPiperazinesPropiolactoneSolubilityCarbamatesCysteinedepalmitoylation probe 5Fluorescent DyesLYPLA1 protein, humanPalmitatespalmostatin BPiperazinesPropiolactonerhodolThiolester HydrolasesWaterXanthones

Identifiers

PMID29023093
PMCPMC5823605
OpenAlexW2760901191

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Registered trials

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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.