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Record W4410529730 · doi:10.1016/j.csbj.2025.05.024

Application of temperature replica exchange molecular dynamics: Structure of mitotic spindle-associated protein SHE1 and its binding to dynein

2025· article· en· W4410529730 on OpenAlexafffund
Laleh Alisaraie, Oliver Stueker, Sayi’Mone Tati

Bibliographic record

VenueComputational and Structural Biotechnology Journal · 2025
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicMicrotubule and mitosis dynamics
Canadian institutionsMemorial University of Newfoundland
FundersNatural Sciences and Engineering Research Council of CanadaAlliance de recherche numérique du Canada
KeywordsReplicaDyneinSpindle apparatusMitosisCell biologyBiophysicsChemistryDynamics (music)Molecular dynamicsBiologyMicrotubulePhysicsBiochemistryCell divisionComputational chemistryCell

Abstract

fetched live from OpenAlex

<h2>Abstract</h2> Cytoskeletal motor protein dynein belongs to the AAA+ superfamily of enzymes, functioning as a mechanochemical ATPase that converts chemical energy into force to drive its retrograde movements along microtubules. Dynein is responsible for cellular cargo transportation; however, viral particles can also recruit dynein. Dynein's mutation is also critical in neurodegenerative and neurodevelopmental diseases. SHE1 is a yeast-specific MT-associated protein that promotes polarizing dynein-mediated spindle movements. Unlike dynein's adaptor proteins, SHE1 is the only protein known to inhibit dynein motility, act independently from dynactin, and alter dynein activity. Despite SHE1's unique mode of action, its structure has not yet been solved experimentally. This work presents the SHE1 structure attained using Temperature Replica Molecular Dynamics simulations. The resulting structure was used to explore the conformations of the complex formed by SHE1 binding to dynein and/or microtubules. The conformations of the complex obtained from the computational protein-protein binding study were clustered using the unsupervised machine learning K-means algorithm. The results helped identify the potential SHE1-dynein interaction sites and the amino acids participating in this interaction, as well as explain the structural details underlying SHE1's potential inhibitory mechanisms. In one of the two main recognized binding sites of SHE1 in the SHE1-dynein complexes, its inhibitory mechanism can be due to its interference with the long-range allosteric communications of dynein's domains, namely strut-stalk-MTBD. In that binding mode, SHE1 can restrain the AAA1/AAA4 modules of the motor ring, affecting its "open-close" conformational changes. That suggests SHE1 could directly interfere with the ATP-hydrolyzing modules necessary for dynein motility. In the second observed binding site, SHE1 interacts with MTBD, α-tubulin, and the C-terminal tail of β-tubulin (E-hook) so that it inhibits the high binding affinity of MTBD to microtubules, preventing its motility, which agrees with the recent <i>in vitro</i> experimental data. Characterizing the SHE1 structure and its complex with SHE1-dynein can serve in the design and development of therapeutic peptide inhibitors of dynein or its mutants for treating dynein-involved diseases.

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 score0.027
Threshold uncertainty score0.525

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 head0.003
GPT teacher head0.225
Teacher spread0.223 · 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 routes2
Has abstractyes

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