Evidence map›Paper›PMID 35680881›Full record

ArticleNature communications2022

Proteomic and functional analyses of the periodic membrane skeleton in neurons.

Ruobo Zhou, Boran Han, Roberta Nowak, Yunzhe Lu, Evan Heller, Chenglong Xia, Athar H Chishti, Velia M Fowler, Xiaowei Zhuang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
13.5field-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

42 citing papers in PubMed, 60 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

9 authors at 4 institutions in 1 country.

Ruobo Zhou *Howard Hughes Medical Institute, Harvard University, Cambridge, MA, 02138, USA. ruobo.zhou@psu.edu.ORCID 0000-0001-8628-0282
Boran Han *Howard Hughes Medical Institute, Harvard University, Cambridge, MA, 02138, USA.ORCID 0000-0001-9567-7062
Roberta NowakDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92307, USA.
Yunzhe LuDepartment of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, MA, 02111, USA.
Evan HellerHoward Hughes Medical Institute, Harvard University, Cambridge, MA, 02138, USA.
Chenglong XiaHoward Hughes Medical Institute, Harvard University, Cambridge, MA, 02138, USA.ORCID 0000-0002-5895-6342
Athar H ChishtiDepartment of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, MA, 02111, USA.
Velia M FowlerDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, 92307, USA.ORCID 0000-0002-3161-8802
Xiaowei ZhuangHoward Hughes Medical Institute, Harvard University, Cambridge, MA, 02138, USA. zhuang@chemistry.harvard.edu.ORCID 0000-0002-6034-7853
Howard Hughes Medical Institute · USScripps Research Institute · USTufts University · USPennsylvania State University · US

Funding

Generation of novel cell type specific mouse genetic toolsU19MH114830 · NIMH · ALLEN INSTITUTE · PI ZENG, HONGKUI · 2017 to 2021
$64.7M
Membrane Skeleton Regulation of Cell Shape and Interactions in Lens DevelopmentR01EY017724 · NEI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2008 to 2024
$6.9M
Deciphering the functional role of actin-spectrin-based membrane skeleton in subcellular compartmentalization of signaling proteins and cell signal transductionR35GM142973 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI ZHOU, RUOBO · 2021 to 2025
$2.2M
Illuminating molecular mechanisms of cellular functions by single-molecule and super-resolution imagingR35GM122487 · NIGMS · HARVARD UNIVERSITY · PI ZHUANG, XIAOWEI · 2017 to 2021
$2.1M
Howard Hughes Medical InstituteNEI NIH HHS R01 EY017724NIGMS NIH HHS R35 GM122487NIGMS NIH HHS R35 GM142973NIMH NIH HHS U19 MH114830
6 · The paper itself

Abstract

Actin, spectrin, and associated molecules form a membrane-associated periodic skeleton (MPS) in neurons. The molecular composition and functions of the MPS remain incompletely understood. Here, using co-immunoprecipitation and mass spectrometry, we identified hundreds of potential candidate MPS-interacting proteins that span diverse functional categories. We examined representative proteins in several of these categories using super-resolution imaging, including previously unknown MPS structural components, as well as motor proteins, cell adhesion molecules, ion channels, and signaling proteins, and observed periodic distributions characteristic of the MPS along the neurites for ~20 proteins. Genetic perturbations of the MPS and its interacting proteins further suggested functional roles of the MPS in axon-axon and axon-dendrite interactions and in axon diameter regulation, and implicated the involvement of MPS interactions with cell adhesion molecules and non-muscle myosin in these roles. These results provide insights into the interactome of the MPS and suggest previously unknown functions of the MPS in neurons.

Indexed as

ProteomicsSpectrinActinsAxonsCell Adhesion MoleculesCell MembraneMembrane ProteinsNeuronsActinsCell Adhesion MoleculesMembrane ProteinsSpectrin

Identifiers

PMID35680881
PMCPMC9184744
OpenAlexW4281725317

What OpenQuestion holds

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LicenceCC BY
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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.