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Record W2264357120 · doi:10.1158/1557-3125.myc15-a12

Abstract A12: Identifying MYC post-translational modifications using a mass spectrometry-based approach

2015· article· en· W2264357120 on OpenAlexaff
Diana Resetca, Manpreet Kalkat, Corey Lourenco, Pak-Kei Chan, Tharan Srikumar, Brian Raught, Linda Z. Penn

Bibliographic record

VenueMolecular Cancer Research · 2015
Typearticle
Languageen
FieldChemistry
TopicAdvanced Proteomics Techniques and Applications
Canadian institutionsPrincess Margaret Cancer CentreUniversity of Toronto
Fundersnot available
KeywordsPhosphorylationSUMO proteinAcetylationThreonineUbiquitinSerineMutantImmunoprecipitationHEK 293 cellsBiologyCarcinogenesisChemistryCell biologyProteasomeCancer researchBiochemistryGene

Abstract

fetched live from OpenAlex

Abstract MYC activity is regulated by a complex network of signaling cascades and protein interactions, some of which result in post-translation modifications (PTMs). For example, phosphorylation of the regulatory threonine 58 (T58) and serine 62 (S62) plays a pivotal role in regulating MYC stability and activity. Loss of this regulatory pathway in cancer can lead to MYC dysregulation and contribute to tumorigenesis. Despite their important role, the majority of MYC PTMs arising downstream of different signaling cascades and their consequences on regulating MYC activity remain largely unknown. To capture the broad spectrum of MYC PTMs, a mass spectrometry (MS)-based approach is being pursued to attain high sequence coverage and enable the identification of PTMs throughout the protein. MYC was overexpressed in the HEK293T cell line, immunoprecipitated, digested, and analyzed on the Velos Orbitrap MS. This analysis facilitated the identification of a range of MYC PTMs, including phosphorylation, sumoylation, ubiquitination and acetylation. Phosphorylation was readily detectable at residues T58 and S62, consistent with previous reports. Additionally, we also observed a previously reported phosphorylation cluster involving residues T343/S344/S347/S348, suggesting that these sites might play a role in regulating MYC function. Indeed, converting these residues to alanine to prevent phosphorylation resulted in a gain-of-function mutant (See Penn Lab poster Lorenco et al.). Another phosphorylation was observed mapping to residues S71 and/or S81. Mutating these sites to alanine also potentiated MYC transformation, highlighting the role of PTMs in regulating MYC function. A MYC sumoylation site was identified on lysine 326 (K326) and is subject of ongoing investigation (See Penn Lab poster Kalkat et al.). Additionally, we will discuss approaches presently underway to increase sequence coverage and identify additional MYC PTMs. PTMs play an important role in regulating the activity of transcription factors, including that of MYC. Moreover, PTMs can contribute to the dysregulation of its activity in cancer. Thus, mapping the array of PTMs in MYC, understanding their role in regulating MYC function, and elucidating the pathways that converge on these PTMs may pave the way for the development of novel therapeutic strategies aimed at targeting MYC-induced tumorigenesis. Citation Format: Diana Resetca, Manpreet Kalkat, Corey Lourenco, Pak-Kei Chan, Tharan Srikumar, Brian Raught, Linda Penn. Identifying MYC post-translational modifications using a mass spectrometry-based approach. [abstract]. In: Proceedings of the AACR Special Conference on Myc: From Biology to Therapy; Jan 7-10, 2015; La Jolla, CA. Philadelphia (PA): AACR; Mol Cancer Res 2015;13(10 Suppl):Abstract nr A12.

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)0.001
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: Methods · Consensus signal: none
Teacher disagreement score0.566
Threshold uncertainty score0.717

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0010.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.001
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.001
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 head0.168
GPT teacher head0.433
Teacher spread0.265 · 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
GenreMethods

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
Published2015
Admission routes1
Has abstractyes

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