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Record W4393167989 · doi:10.1016/j.jbc.2024.107069

Abstract 2237 Cryo-EM analysis of scorpion toxin binding to Ryanodine Receptors reveals sub-conductance that is abolished by PKA phosphorylation

2024· article· en· W4393167989 on OpenAlexafffundabout
Omid Haji‐Ghassemi, Filip Van Petegem, Héctor H. Valdivia, Seby Chen, Kellie A. Woll, Giorgina Gurrola, Carmen R. Valdivia, Wenxuan Cai, Songhua Li

Bibliographic record

VenueJournal of Biological Chemistry · 2024
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicIon channel regulation and function
Canadian institutionsUniversity of Calgary
FundersCanadian Institutes of Health ResearchChapman UniversityNational Institutes of HealthMichael Smith Health Research BCNational Science Foundation
KeywordsRyanodine receptorPhosphorylationScorpionToxinReceptorChemistryConductanceBiophysicsBiochemistryBiologyPhysicsVenom

Abstract

fetched live from OpenAlex

We recently elucidated the interaction between scorpion venom-derived calcins and intracellular Ryanodine Receptors (RyRs). The study primarily focuses on uncovering the structural and functional dynamics of this interaction, leveraging cryo-electron microscopy (cryo-EM) for detailed insights. We analyzed the binding mechanism of calcins, small peptides from scorpion venom, to RyRs using a combination of single particle cryo-EM and electrophysiology. These channels, located within the endoplasmic and sarcoplasmic reticulum, play a crucial role in calcium ion flow. Our approach includes structural mapping of toxin-channel interaction, assessment of conductivity changes, and exploring the impact of post-translational modifications on toxin functionality. Results indicate that calcins bind within the RyR's cytosolic shell, near the transmembrane region, inducing a sub-conductance state. This binding elongates the ion conduction pathway, reducing the channel's conductivity. Notably, this study is the first to demonstrate the asymmetric conformational changes in RyRs upon toxin binding, which significantly affects subunit interactions. Additionally, we discovered that PKA phosphorylation of calcins prevents their binding to RyRs, highlighting a unique interplay between the toxin and intracellular enzymes. The conclusions drawn from this study are multi-fold: First, the observed binding mechanism of calcins offers a structural template for designing potent RyR blockers, potentially beneficial in treating disorders like heart failure and Alzheimer's disease. Second, the asymmetric conformational changes induced by calcins provide novel insights into the structural dynamics of RyRs. Lastly, the modulation of calcin function through PKA phosphorylation unveils a critical regulatory mechanism, suggesting a balance between kinase and phosphatase activities determines the functional outcome in cellular contexts. This work was funded by Canadian Institutes of Health Research grant PJT-159601 (F.V.P.), Canadian Institutes of Health Research fellowship MFE-381863 (O.H.-G.), Michael Smith Foundation for Health Research fellowship (O.H.-G.), Fonds de Recherche du Québec–Santé fellowship BF7-310636 (Y.S.C.), and National Institutes of Health grant R01-HL055438.

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: Not applicable · Consensus signal: none
GenreCandidate signal: Other · Consensus signal: none
Teacher disagreement score0.002
Threshold uncertainty score0.006

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 integrity0.0000.001
Insufficient payload (model declined to judge)0.0020.000

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 head0.024
GPT teacher head0.269
Teacher spread0.245 · 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 designNot applicable
Domainnot available
GenreOther

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
Published2024
Admission routes3
Has abstractyes

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