Evidence map›Paper›PMID 38456967›Full record

ArticleThe Journal of cell biology2024

Multivalent coiled-coil interactions enable full-scale centrosome assembly and strength.

Manolo U Rios, Małgorzata A Bagnucka, Bryan D Ryder, Beatriz Ferreira Gomes, Nicole E Familiari, Kan Yaguchi, Matthew Amato, Weronika E Stachera, Łukasz A Joachimiak, Jeffrey B Woodruff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
9.5field-weighted citation impact, top 1% of its field
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

22 citing papers in PubMed, 31 citations in OpenAlex.

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  17. Polo-like kinase 1 prevents excess microtubule polymerization inbioRxiv : the preprint server for biology · 2024
    Article
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  19. Cep57 regulates human centrosomes through multivalent interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Manolo U RiosDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0001-8457-5378
Małgorzata A Bagnucka *Department of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-4363-0796
Bryan D Ryder *Department of Biochemistry, Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0003-1393-0875
Beatriz Ferreira Gomes *Max Planck Institute of Molecular Cell Biology and Genetics , Dresden, Germany.ORCID 0000-0002-7610-9630
Nicole E FamiliariDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0009-0007-2282-5563
Kan YaguchiDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-8348-587X
Matthew AmatoDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-5768-5237
Weronika E StacheraDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-1753-4098
Łukasz A JoachimiakDepartment of Biochemistry, Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0003-3061-5850
Jeffrey B WoodruffDepartment of Cell Biology, Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.ORCID 0000-0002-5590-9620
The University of Texas Southwestern Medical Center · USSouthwestern Medical Center · USMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
Seeds and Strains Derived from Tau Monomer - Perez Diversity SupplementRF1AG065407 · NIA · UT SOUTHWESTERN MEDICAL CENTER · PI DIAMOND, MARC I, JOACHIMIAK, LUKASZ A. · 2020 to 2021
$3.2M
Molecular, material, and structural design principles of centrosomesR35GM142522 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Jeffrey B Woodruff · 2021 to 2026
$2.5M
Molecular Biophysics Training ProgramT32GM131963 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI Luke W Rice · 2019 to 2026
$1.5M
OneMP Mass PhotometerS10OD030312 · OD · UT SOUTHWESTERN MEDICAL CENTER · PI BRAUTIGAM, CHAD · 2021 to 2021
$165k
NIA NIH HHS RF1 AG065407NIGMS NIH HHS 1R35GM142522NIGMS NIH HHS R35 GM142522NIGMS NIH HHS T32 GM007062NIGMS NIH HHS T32 GM131963NIH HHS 1RF1AG065407-01A1NIH HHS S10 OD030312
6 · The paper itself

Abstract

The outermost layer of centrosomes, called pericentriolar material (PCM), organizes microtubules for mitotic spindle assembly. The molecular interactions that enable PCM to assemble and resist external forces are poorly understood. Here, we use crosslinking mass spectrometry (XL-MS) to analyze PLK-1-potentiated multimerization of SPD-5, the main PCM scaffold protein in C. elegans. In the unassembled state, SPD-5 exhibits numerous intramolecular crosslinks that are eliminated after phosphorylation by PLK-1. Thus, phosphorylation induces a structural opening of SPD-5 that primes it for assembly. Multimerization of SPD-5 is driven by interactions between multiple dispersed coiled-coil domains. Structural analyses of a phosphorylated region (PReM) in SPD-5 revealed a helical hairpin that dimerizes to form a tetrameric coiled-coil. Mutations within this structure and other interacting regions cause PCM assembly defects that are partly rescued by eliminating microtubule-mediated forces, revealing that PCM assembly and strength are interdependent. We propose that PCM size and strength emerge from specific, multivalent coiled-coil interactions between SPD-5 proteins.

Indexed as

Caenorhabditis elegansCell Cycle ProteinsCentrosomePolo-Like Kinase 1AnimalsCaenorhabditis elegans ProteinsMicrotubulesCaenorhabditis elegans ProteinsCell Cycle Proteinsplk-1 protein, C elegansPolo-Like Kinase 1SPD-5 protein, C elegans

Identifiers

PMID38456967
PMCPMC10921949
OpenAlexW4392594745

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.