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Record W4416008059 · doi:10.1016/j.jbc.2025.110921

C-spine mutations of protein kinase C and Akt as a novel generalizable approach to create stable pseudokinases

2025· article· en· W4416008059 on OpenAlexfundno aff
Stefanie Hodapp, Tiffany Kao, Jian Wu, Nileeka Balasuriya, Corina E. Antal, Susan S. Taylor, Alexandra C. Newton

Bibliographic record

VenueJournal of Biological Chemistry · 2025
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Kinase Regulation and GTPase Signaling
Canadian institutionsnot available
FundersNational Center for Advancing Translational SciencesNational Heart, Lung, and Blood InstituteNational Institute of General Medical SciencesNatural Sciences and Engineering Research Council of CanadaUniversity of California, San DiegoNational Institutes of Health
KeywordsAutophosphorylationMutantKinaseProtein kinase APhosphorylationProtein kinase CAdenosine kinaseMutationProtein kinase B

Abstract

fetched live from OpenAlex

Protein kinases function not only through their catalytic phospho-transfer activity but also by noncatalytic scaffold mechanisms. Introduction of mutations to inactivate catalysis provides a tool to differentiate between the two; however, kinase-inactivating mutations may alter the structure of the kinase domain and perturb scaffold functions. Here, we developed a strategy that prevents ATP binding, thereby preventing catalysis, while stabilizing the active conformation of the kinase domain. This approach leverages the structural role of ATP in assembling the catalytic spine (C-spine), a hydrophobic core essential for the active conformation. Specifically, we substituted Val or Ala residues proximal to the binding position of the adenosine ring of ATP with Phe in three protein kinase C isozymes (PKCβII, γ, and θ) and Akt1. Structural modeling suggests that Phe substitutions at these positions are a surrogate for the adenosine ring of ATP to assemble the C-spine. Live-cell imaging using genetically encoded PKC and Akt activity reporters reveals that C-spine mutations abolish kinase activity. Furthermore, phosphorylation of the hydrophobic motif, an autophosphorylation site, is abolished in C-spine mutants of PKC family members and reduced in C-spine mutants of Akt1, independent of epidermal growth factor stimulation. In PKCβII, these C-spine mutations accelerate plasma membrane translocation, consistent with impaired autoinhibition due to the lack of hydrophobic motif phosphorylation. Despite adopting reduced autoinhibition, turnover experiments with PKCθ reveal C-spine mutants do not impair the stability of the full-length PKC. The generation of pseudokinases by C-spine mutations provides a generalizable strategy for elucidating noncatalytic kinase functions.

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 score0.007
Threshold uncertainty score0.441

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 head0.019
GPT teacher head0.265
Teacher spread0.246 · 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

Citations2
Published2025
Admission routes1
Has abstractyes

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