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Regulation of N‐myristoyltransferase by Akt/PKB Mediated Phosphorylation

2016· article· en· W4389026707 on OpenAlexaffabout
Sujeet Kumar, Rajendra K. Sharma

Bibliographic record

VenueThe FASEB Journal · 2016
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Kinase Regulation and GTPase Signaling
Canadian institutionsUniversity of Saskatchewan
Fundersnot available
KeywordsPhosphorylationProtein kinase BBiochemistryKinaseBiologyCell biologyBinding sitePeptideProtein kinase AChemistry

Abstract

fetched live from OpenAlex

Post‐translational modifications of proteins create highly dynamic relay system that regulates the core dynamic signalling pathways in response to the alterations in the cellular microenvironment. N‐myristoyltransferase (NMT) has emerged as a central node upstream of diverse signalling proteins regulating cellular survival. NMT modifies proteins in both co‐and post‐translational manner and modulates functioning of the signalling proteins by addition of the myristoyl moiety to an exposed N‐terminal glycine. The sequence feature of NMT reflects that it harbours an Akt/PKB kinase recognition motif within the aD‐ aE loop region. The in vitro kinase assay on the synthetic peptides corresponding to the aD‐aE loop followed by MALDI‐MS analysis established that the sequence motif is a valid substrate for the Akt/PKB kinase. The MS‐MS analysis of the phosphorylated peptide identified Thr319 within aD‐ aE loop region as the site of phosphorylation. To delineate the effects of phosphorylation, phosphomimetic mutant (Thr319Glu) and a null‐mutant (Thr319Ala) were engineered onto the catalytic domain the NMT. Enzymatic assays of the purified recombinant enzymes reflected a drastic loss in activity by mutations at the site Thr319. The analysis of NMT crystal structures shows that this loop region undergoes a conformational change upon binding of the co‐substrate myristoyl‐CoA (MYA). The binding of peptide substrate follows the MYA binding event and Thr319 in the aD‐ aE loop region lies in proximity to the peptide‐substrate binding site. In summary, we have established the site of phosphorylation and the regulation of NMT by the kinase Akt/PKB. These findings indicate that Akt/PKB kinase restricts NMT activity by modulating the peptide substrate affinity presumably by changing in the interaction network around the substrate‐binding site. Delineating of the functional consequences of this novel phosphorylation event is expected to improve our understanding of NMT regulations in diversified cellular needs. Support or Funding Information This work was supported by the Canadian Breast Cancer Foundation‐Prairies/NWT operating grant to RKS (Grant number ‐ 412572).

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 machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation 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 score0.001
Threshold uncertainty score0.004

Distilled classifier scores by category (both heads)

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)0.0010.000

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 head0.218
Teacher spread0.210 · 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 source (direct Gemma or distilled Codex), 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
Published2016
Admission routes2
Has abstractyes

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