Evidence map›Paper›PMID 35819332›Full record

ArticleThe Journal of cell biology2022

IRSp53 promotes postsynaptic density formation and actin filament bundling.

Zhe Feng, Suho Lee, Bowen Jia, Tao Jian, Eunjoon Kim, Mingjie Zhang

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Zhe FengDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.
Suho LeeCenter for Synaptic Brain Dysfunctions, Institute for Basic Science (IBS), Daejeon, Korea.
Bowen JiaDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID 0000-0002-2862-6625
Tao JianDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID 0000-0002-9754-1051
Eunjoon KimCenter for Synaptic Brain Dysfunctions, Institute for Basic Science (IBS), Daejeon, Korea.ORCID 0000-0001-5518-6584
Mingjie ZhangDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID 0000-0001-9404-0190
Hong Kong University of Science and Technology · HKInstitute for Basic Science · KRKorea Advanced Institute of Science and Technology · KR

Funding

General Research Fund of RGC 16102120Hong Kong University of Science and TechnologyHuman Frontier Science Program RGP0020/2019Institute of Basic Science IBS-R002-D1Ministry of Science and Technology of China 2019YFA0508402National Natural Science Foundation of China 82188101RGC of Hong Kong AoE-M09-12
6 · The paper itself

Abstract

IRSp53 (aka BAIAP2) is a scaffold protein that couples membranes with the cytoskeleton in actin-filled protrusions such as filopodia and lamellipodia. The protein is abundantly expressed in excitatory synapses and is essential for synapse development and synaptic plasticity, although with poorly understood mechanisms. Here we show that specific multivalent interactions between IRSp53 and its binding partners PSD-95 or Shank3 drive phase separation of the complexes in solution. IRSp53 can be enriched to the reconstituted excitatory PSD (ePSD) condensates via bridging to the core and deeper layers of ePSD. Overexpression of a mutant defective in the IRSp53/PSD-95 interaction perturbs synaptic enrichment of IRSp53 in mouse cortical neurons. The reconstituted PSD condensates promote bundled actin filament formation both in solution and on membranes, via IRSp53-mediated actin binding and bundling. Overexpression of mutants that perturb IRSp53-actin interaction leads to defects in synaptic maturation of cortical neurons. Together, our studies provide potential mechanistic insights into the physiological roles of IRSp53 in synapse formation and function.

Indexed as

ActinsNerve Tissue ProteinsPost-Synaptic DensityActin CytoskeletonAnimalsMiceMicrofilament ProteinsNeuronal PlasticityNeuronsPseudopodiaSynapsesActinsBaiap2 protein, mouseMicrofilament ProteinsNerve Tissue ProteinsShank3 protein, mouse

Identifiers

PMID35819332
PMCPMC9280192
OpenAlexW4285076447

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.