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Record W4411569222 · doi:10.1002/pmic.13980

Covalent Inhibition of the Peptidyl‐Prolyl Isomerase Pin1 by Sulfopin Results in a Broad Impact on the Phosphoproteome of Human Osteosarcoma U2‐OS Cells

2025· article· en· W4411569222 on OpenAlexafffund
Scott E. Roffey, Owen Hovey, Kristina Jurčić, Kun Ping Lu, Xiao Zhen Zhou, David W. Litchfield

Bibliographic record

VenuePROTEOMICS · 2025
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicSignaling Pathways in Disease
Canadian institutionsWestern University
FundersNatural Sciences and Engineering Research Council of CanadaCanadian Institutes of Health ResearchCanada Foundation for InnovationOntario Institute for Cancer Research
KeywordsPIN1OsteosarcomaIsomeraseChemistryBiochemistryCovalent bondPosttranslational modificationComputational biologyProlyl isomeraseBiologyEnzymeCancer researchOrganic chemistry

Abstract

fetched live from OpenAlex

Peptidyl-prolyl isomerase, NIMA-interacting protein 1-(Pin1) catalyses the cis-trans interconversion of the inflexible bond between serine or threonine residues and proline at the +1 position (pSer/pThr-Pro). Although initially discovered as an essential regulator of cell division, Pin1 has since been identified as a regulator of many biological processes and is associated with numerous malignancies and neurodegenerative disorders. Pin1 has been shown to influence phosphorylation by modulating phosphatase accessibility. However, it can also indirectly regulate phosphorylation by isomerizing peptidyl-prolyl bonds on kinases, affecting their subcellular localization and/or substrate specificity. Here, SILAC-based mass spectrometry was employed to identify proteomic and phosphoproteomic changes in human osteosarcoma human osteosarcoma cell line (U2-OS) cells in response to treatment with the selective covalent Pin1 inhibitor Sulfopin. We confirmed that Sulfopin covalently binds Pin1 and profiled Pin1-dependent changes to the proteome and phosphoproteome, identifying 803 phosphosites that underwent significant Sulfopin-dependent changes. The identified phosphosites include substrates for a number of distinct kinases, including protein kinase B (AKT1), aurora kinase A (AURKA), cyclin-dependent kinase (CDK)1 and CK2. Overall, this study reveals the broad impact of Sulfopin on the phosphoproteome, improving our understanding of how Pin1 modulates complex regulatory kinase networks in living cells. SUMMARY: The peptidyl-prolyl isomerase (PPIase) Pin1 has emerged as a potential therapeutic target for numerous malignancies and neurodegenerative disorders based on its altered expression in several diseases. As the activity of Pin1 is phosphorylation-dependent, it is intimately involved with constituents of regulatory kinase networks within cells. To elucidate how Pin1 orchestrates regulatory signalling within cells, we performed quantitative proteomic and phosphoproteomic profiling of SILAC-labelled human osteosarcoma U2-OS cells treated with Sulfopin, a highly selective covalent Pin1 inhibitor. In addition to demonstrating that Pin1 inhibition alters the abundance and phosphorylation of proteins involved in a variety of fundamental cellular processes, these studies revealed that Pin1 inhibition modulates the phosphorylation of 803 phosphorylation sites, ultimately improving our understanding of how a PPIase regulates phosphorylation networks in complex biological systems.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.003
Threshold uncertainty score0.564

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.008
GPT teacher head0.258
Teacher spread0.250 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2025
Admission routes2
Has abstractyes

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