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Record W2228305482 · doi:10.3892/mmr.2015.4718

Inhibition of E-cadherin/catenin complex formation by O-linked N-acetylglucosamine transferase is partially independent of its catalytic activity

2015· article· en· W2228305482 on OpenAlexfundno aff
Haiyan Liu, Yuchao Gu, Jieqiong Qi, Cuifang Han, Xinling Zhang, Chuanlin Bi, Wengong Yu

Bibliographic record

VenueMolecular Medicine Reports · 2015
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicGlycosylation and Glycoproteins Research
Canadian institutionsnot available
FundersSimon Fraser UniversityNational Natural Science Foundation of ChinaBarbara Ann Karmanos Cancer InstituteVanderbilt University Medical CenterYonsei UniversityWayne State UniversityVanderbilt University
KeywordsCateninImmunoprecipitationCadherinMutantCytoplasmBiologyCell biologyTransferaseCell adhesionBiochemistryMolecular biologyChemistryCellEnzymeSignal transductionGene

Abstract

fetched live from OpenAlex

p120-catenin (p120) contains a large central armadillo repeat domain, via which it binds to E‑cadherin to stabilize the latter, thereby regulating cell‑to‑cell adhesion. A previous study by our group demonstrated that O‑linked N‑acetylglucosamine (O‑GlcNAc) is involved in the regulation of the interaction between p120 and E‑cadherin. As O‑GlcNAc transferase (OGT) is able to directly bind to the majority of its target proteins, the present study hypothesized that OGT may additionally regulate the formation of the E‑cadherin/catenin complex independent of its catalytic activity. To verify this hypothesis, a catalytically inactive OGT mutant was expressed in H1299 cells, and its effects on the formation of the E‑cadherin/catenin complex were assessed. A cytoskeleton‑binding protein extraction assay confirmed that OGT inhibited the formation of the E‑cadherin/catenin complex independent of its catalytic activity. In addition, co‑immunoprecipitation and pull‑down assays were used to evaluate the interaction between OGT and p120. Immunoblotting indicated that OGT was able to directly bind to p120. To determine the domain of p120 involved in binding to OGT, a series of deletion mutants of p120 were constructed and subjected to protein binding assays by pull‑down assays. Immunoblotting showed that OGT bound to the regulatory and armadillo domains of p120, which might interfere with the interaction between p120 and E‑cadherin. Finally, OGT, p120 and E‑cadherin cytoplasmic domains (ECD) were recombinantly expressed in BL21 (DE3) recombinant E. coli cells, and a glutathione S‑transferase (GST) pull‑down assay was performed to assess the interactions among the purified recombinant proteins. Immunoblotting indicated that maltose‑binding protein (MBP)‑OGT inhibited the binding of His‑p120 to GST‑ECD in a dose‑dependent manner. All of these results suggested that OGT inhibited the formation of the E‑cadherin/catenin complex through reducing the interaction between p120 and E‑cadherin. The present study provided a novel underlying mechanism of the regulation of the interaction between p120 and E‑cadherin, and thus E‑cadherin‑mediated cell‑cell adhesion, which has essential roles in cancer development and progression.

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: Empirical · Consensus signal: Empirical
Teacher disagreement score0.023
Threshold uncertainty score0.630

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0010.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
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 head0.039
GPT teacher head0.304
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
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

Citations8
Published2015
Admission routes1
Has abstractyes

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