Evidence map›Paper›PMID 36037369›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Nucleation of the destruction complex on the centrosome accelerates degradation of β-catenin and regulates Wnt signal transmission.

Ryan S Lach, Chongxu Qiu, Erfan Zeyaei Kajbaf, Naomi Baxter, Dasol Han, Alex Wang, Hannah Lock, Orlando Chirikian, Beth Pruitt, Maxwell Z Wilson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Article
  2. Review
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  6. Article
  7. Proofreading and single-molecule sensitivity in T cell receptor signaling by condensate nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
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  11. Article
  12. Review
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  14. Review
  15. To condense or not to condense: Wnt regulation by centrosome-nucleated biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Ryan S LachDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0003-2846-618X
Chongxu QiuDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0001-8418-5898
Erfan Zeyaei KajbafDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
Naomi BaxterDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0001-9249-9184
Dasol HanNeuroscience Research Institute, University of California, Santa Barbara, CA 93106.
Alex WangDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.
Hannah LockDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0002-3282-7454
Orlando ChirikianBiomolecular Science and Engineering, University of California, Santa Barbara, CA 93106.
Beth PruittDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0002-4861-2124
Maxwell Z WilsonDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA 93106.ORCID 0000-0003-0768-7004

Funding

A New Phase of Wnt: Interrogating a Thermodynamic Signaling Node Using OptogeneticsF31HD106900 · NICHD · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI LACH, RYAN · 2021 to 2023
$139k
NICHD NIH HHS F31 HD106900
6 · The paper itself

Abstract

Wnt signal transduction is controlled by the destruction complex (DC), a condensate comprising scaffold proteins and kinases that regulate β-catenin stability. Overexpressed DC scaffolds undergo liquid-liquid phase separation (LLPS), but DC mesoscale organization at endogenous expression levels and its role in β-catenin processing were previously unknown. Here, we find that DC LLPS is nucleated by the centrosome. Through a combination of CRISPR-engineered custom fluorescent tags, finite element simulations, and optogenetic tools that allow for manipulation of DC concentration and multivalency, we find that centrosomal nucleation drives processing of β-catenin by colocalizing DC components to a single reaction crucible. Enriching GSK3β partitioning on the centrosome controls β-catenin processing and prevents Wnt-driven embryonic stem cell differentiation to mesoderm. Our findings demonstrate the role of nucleators in controlling biomolecular condensates and suggest tight integration between Wnt signal transduction and the cell cycle.

Indexed as

beta CateninCentrosomeEmbryonic Stem CellsWnt Signaling PathwayCell DifferentiationClustered Regularly Interspaced Short Palindromic RepeatsGlycogen Synthase Kinase 3 betaMesodermbeta CateninGlycogen Synthase Kinase 3 betadestruction complexLLPSoptogeneticsstem cellsWnt

Identifiers

PMID36037369
PMCPMC9457612

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.