Evidence map›Paper›PMID 39674848›Full record

ArticleJournal of muscle research and cell motility2025

Numb family proteins play roles in Desmin and Vimentin localization at the Z-disc.

Baolei Wang, Shujuan Li, Yan Yang, Jinfeng Luo

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Article in Journal of muscle research and cell motility, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Baolei WangWest China Developmental & Stem Cell Biology Institute, West China Second University Hospital, Sichuan University, Chengdu, 610041, Sichuan, China. 1000wy@163.com.
Shujuan LiChildren's Hospital Affiliated to Zhengzhou University, Zhengzhou, 450018, Henan, China.
Yan YangWest China Developmental & Stem Cell Biology Institute, West China Second University Hospital, Sichuan University, Chengdu, 610041, Sichuan, China.
Jinfeng LuoWest China Developmental & Stem Cell Biology Institute, West China Second University Hospital, Sichuan University, Chengdu, 610041, Sichuan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Desmin and Vimentin are major intermediate filaments at the Z-disc and play significant roles in sarcomere architecture and signaling transduction. Abnormal expression of sarcomeric Desmin and Vimentin (SDV) results in severe dysfunctions of striated muscles. In this study, it was found that paired Numb family proteins (NFPs), including Numb and its homolog Numblike, determined the range for the recruitment of SDV to the primitive Z-disc. Notably, NFPs were identified as SDV associated proteins and bound to the head, rod, and tail domains of SDV in a splicing-variant-dependent manner. Last, the construction and consolidation of the Z-disc was completed through the gradual adjustment of the position of SDV by clockwise/anticlockwise rotation of paired NFPs to 90° in the same direction. Conditional knockout of NFPs altered the arrangement and accumulated the expression level of SDV. This study further enriches the functions of NFPs in sarcomere assembly and maintenance through cooperation with SDV.

Indexed as

DesminMembrane ProteinsNerve Tissue ProteinsSarcomeresVimentinAnimalsHumansIntermediate FilamentsMiceDesminMembrane ProteinsNerve Tissue ProteinsNumb protein, mouseVimentinDesminheartNumbsarcomereVimentinZdisc

Identifiers

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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.