Evidence map›Paper›PMID 38727267›Full record

ReviewCells2024

Pin1-Catalyzed Conformation Changes Regulate Protein Ubiquitination and Degradation.

Jessica Jeong, Muhammad Usman, Yitong Li, Xiao Zhen Zhou, Kun Ping Lu

Abstract readReview
In one paragraph

Review in Cells, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Epigenomic profile of GBA1 in Parkinson's disease.Parkinsonism & related disorders · 2025
    Article
  6. Review
  7. Article
  8. Review
  9. Pin1 promotes human CaCell communication and signaling : CCS · 2024
    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.

Jessica JeongDepartments of Biochemistry and Oncology, Schulich School of Medicine & Dentistry, Western University, London, ON N6A 5C1, Canada.
Muhammad UsmanDepartments of Biochemistry and Oncology, Schulich School of Medicine & Dentistry, Western University, London, ON N6A 5C1, Canada.
Yitong LiDepartments of Biochemistry and Oncology, Schulich School of Medicine & Dentistry, Western University, London, ON N6A 5C1, Canada.
Xiao Zhen ZhouDepartments of Biochemistry and Oncology, Schulich School of Medicine & Dentistry, Western University, London, ON N6A 5C1, Canada.
Kun Ping LuDepartments of Biochemistry and Oncology, Schulich School of Medicine & Dentistry, Western University, London, ON N6A 5C1, Canada.ORCID 0000-0002-0734-1567

Funding

CIHR 502128CIHR 506475CIHR 506500
6 · The paper itself

Abstract

The unique prolyl isomerase Pin1 binds to and catalyzes cis-trans conformational changes of specific Ser/Thr-Pro motifs after phosphorylation, thereby playing a pivotal role in regulating the structure and function of its protein substrates. In particular, Pin1 activity regulates the affinity of a substrate for E3 ubiquitin ligases, thereby modulating the turnover of a subset of proteins and coordinating their activities after phosphorylation in both physiological and disease states. In this review, we highlight recent advancements in Pin1-regulated ubiquitination in the context of cancer and neurodegenerative disease. Specifically, Pin1 promotes cancer progression by increasing the stabilities of numerous oncoproteins and decreasing the stabilities of many tumor suppressors. Meanwhile, Pin1 plays a critical role in different neurodegenerative disorders via the regulation of protein turnover. Finally, we propose a novel therapeutic approach wherein the ubiquitin-proteasome system can be leveraged for therapy by targeting pathogenic intracellular targets for TRIM21-dependent degradation using stereospecific antibodies.

Indexed as

NIMA-Interacting Peptidylprolyl IsomeraseProteolysisUbiquitinationAnimalsHumansNeoplasmsNeurodegenerative DiseasesProtein ConformationUbiquitin-Protein LigasesNIMA-Interacting Peptidylprolyl IsomerasePIN1 protein, humanUbiquitin-Protein Ligasescancercis–trans conformational changesE3 ligaseneurodegenerationphosphorylation signalingPin1protein ubiquitinationproteosome pathwayTRIM21

Identifiers

PMID38727267
PMCPMC11083468

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.