Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Aug 28;13:14054. doi: 10.1038/s41598-023-41008-5

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Alteration of agrin- mediated MuSK signaling induced by mutation in LRP4. (A) The LRP4 mutant inhibits agrin binding in vitro. HEK293T cells were transfected with wild-type (WT) or mutant (Mut) LRP4-HA plasmids. After immunoprecipitation of LRP4-HA and incubation with or without neural agrin (1 μg/ml), the level of agrin binding to LRP4 is followed by immunobloting with anti-agrin antibody. Lines indicate that intervening lanes have been spliced out. (B) Agrin binding to LRP4 shows a significant impairment of agrin binding to LRP4 mutated in vitro. (C) The LRP4 mutant does not affect its binding to its coreceptor MuSK. After co-expression of MuSK-Flag and LRP4-HA in HEK293T cells and immunoprecipitation of MuSK-Flag or LRP4-HA with anti-Flag and anti-HA respectively, the level of MuSK or LRP4 is followed by immunoblotting with anti-Flag or anti-HA antibodies. (D) LRP4 binding to MuSK doesn’t show significant changes of LRP4/MuSK binding when LRP4 is mutated in vitro. (E) The mutation in LRP4 inhibits agrin-mediated regulation of MuSK phosphorylation. HEK293T cells were transfected with MuSK-Flag and WT LRP4-HA or mutant LRP4-HA with or without agrin (0.4 μg/ml) for various times (1, 3 or 6 h). Phosphorylated MuSK was detected by immunoprecipitation of MuSK-Flag and followed by immunoblotting with anti-4G10 (MuSK phosphorylation), anti-Flag and anti-HA antibodies. Lines indicate that intervening lanes have been spliced out. (F) MuSK phosphorylation induced by agrin is significantly impaired when LRP4 is mutated in vitro. p < 0.05, Student’s test. N = 3 blots for each condition. Source data are provided as a Source Data file.