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Spatiotemporal Organization Of Signaling: From Plasma Membrane To Chromatin

2016· article· en· W4389027546 on OpenAlexafffundabout
Anne‐Claude Gingras

Bibliographic record

VenueThe FASEB Journal · 2016
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicBiotin and Related Studies
Canadian institutionsLunenfeld-Tanenbaum Research InstituteUniversity of Toronto
FundersNatural Sciences and Engineering Research Council of Canada
KeywordsBiotinylationOrganelleCell biologyCellular compartmentCompartmentalization (fire protection)BiologyProtein subcellular localization predictionSubcellular localizationComputational biologyCompartment (ship)Transport proteinNucleic acidCell signalingChemistryBiochemistryCellSignal transductionCytoplasm

Abstract

fetched live from OpenAlex

Compartmentalization is essential for all complex forms of life. In eukaryotic cells, membrane‐bound organelles, as well as a multitude of protein‐ and nucleic acid‐rich subcellular structures, maintain boundaries and serve as enrichment zones to promote and regulate protein function. Consistent with the critical importance of these boundaries, alterations in the machinery that mediate protein transport between these compartments has been implicated in a number of diverse diseases. Signaling molecules are no exception, and must be targeted to specific locations for proper activation in time and place. Understanding the composition of each cellular “compartment” (be it a classical organelle or a large protein complex) remains a challenging task. For soluble protein complexes, approaches such as affinity purification other biochemical fractionation coupled to mass spectrometry provides important insight, including on the temporal regulation of signaling, but this is not the case for detergent‐insoluble components. Classically, both microscopy and organellar purifications have been employed for identifying the composition of these structures, but these approaches have limitations, notably in resolution for standard high‐throughput fluorescence microscopy and in the difficulty in purifying some of the structures (e.g. p‐bodies) for approaches based on biochemical isolations. Prompted by the recent implementation in vivo biotinylation approaches such as BioID, we have begun the systematic mapping of the composition of various subcellular structures, using as baits proteins (or protein fragments) which are well‐characterized markers for a specified location. We report here our low‐resolution map of a human cell (currently defined from BioID profiling of 100 marker proteins), including various membrane compartments, cytoskeletal structures and nuclear subdomains. We will also introduce a higher resolution map of RNA‐containing cellular structures, including the p‐bodies and the stress granules that regulate mRNA stability, and new data on signaling pathways that span insoluble compartments. We demonstrate in vivo biotinylation to be a scalable approach capable of revealing protein complexes as well as their association into larger structures. Support or Funding Information Work in the Gingras lab was primarily supported by the Canadian Institutes for Health Research (Foundation grant) and the Natural Sciences and Engineering Research Council of Canada (Discovery grant). Additional funding was provided by Genome Canada through Ontario Genomics.

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 score0.004
Threshold uncertainty score0.136

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 head0.008
GPT teacher head0.214
Teacher spread0.206 · 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

Citations0
Published2016
Admission routes3
Has abstractyes

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