Evidence map›Paper›PMID 39150071›Full record

ArticleProtein science : a publication of the Protein Society2024

Dissecting the functional behavior of the differentially phosphorylated prolyl isomerase, Pin1.

Danielle F Kay, Adem Ozleyen, Cristina Matas De Las Heras, Richard G Doveston, Aneika C Leney

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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.

Danielle F KaySchool of Biosciences, University of Birmingham, Edgbaston, UK.ORCID 0000-0001-9559-7388
Adem OzleyenLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.ORCID 0000-0003-0195-3383
Cristina Matas De Las HerasLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.ORCID 0009-0000-7205-986X
Richard G DovestonLeicester Institute of Structural and Chemical Biology, University of Leicester, Leicester, UK.ORCID 0000-0002-7399-9607
Aneika C LeneySchool of Biosciences, University of Birmingham, Edgbaston, UK.ORCID 0000-0002-2066-4950

Funding

BBSRC BB/S019456/1BBSRC BB/T000746X/1Ministry of National Education of the Republic of Türkiye
6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) play an intricate role in a diverse range of cellular processes creating a complex PTM code that governs cell homeostasis. Understanding the molecular build-up and the critical factors regulating this PTM code is essential for targeted therapeutic design whereby PTM mis-regulation is prevalent. Here, we focus on Pin1, a peptidyl-prolyl cis-trans isomerase whose regulatory function is altered by a diverse range of PTMs. Through employing advanced mass spectrometry techniques in combination with fluorescence polarization and enzyme activity assays, we elucidate the impact of combinatorial phosphorylation on Pin1 function. Moreover, two phosphorylation sites were identified whereby Ser71 phosphorylation preceded Ser16 phosphorylation, leading to the deactivation of Pin1's prolyl isomerase activity before affecting substrate binding. Together, these findings shed light on the regulatory mechanisms underlying Pin1 function and emphasize the importance of understanding PTM landscapes in health and disease.

Indexed as

NIMA-Interacting Peptidylprolyl IsomeraseHumansPhosphorylationProtein Processing, Post-TranslationalNIMA-Interacting Peptidylprolyl IsomerasePIN1 protein, humannative mass spectrometryphosphorylationpost‐translational modificationsprolyl isomeraseproteomics

Identifiers

PMID39150071
PMCPMC11328113

What OpenQuestion holds

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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.