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POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan
Journal article   Open access   Peer reviewed

POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan

Ameya S Walimbe, Hidehiko Okuma, Soumya Joseph, Tiandi Yang, Takahiro Yonekawa, Jeffrey M Hord, David Venzke, Mary E Anderson, Silvia Torelli, Adnan Manzur, …
eLife, Vol.9, e61388
09/25/2020
DOI: 10.7554/eLife.61388
PMCID: PMC7556876
PMID: 32975514
url
https://doi.org/10.7554/eLife.61388View
Published (Version of record) Open Access

Abstract

Matriglycan [-GlcA-β1,3-Xyl-α1,3-] serves as a scaffold in many tissues for extracellular matrix proteins containing laminin-G domains including laminin, agrin, and perlecan. Like-acetyl-glucosaminyltransferase 1 (LARGE1) synthesizes and extends matriglycan on α-dystroglycan (α-DG) during skeletal muscle differentiation and regeneration; however, the mechanisms which regulate matriglycan elongation are unknown. Here, we show that Protein -Mannose Kinase (POMK), which phosphorylates mannose of core M3 (GalNAc-β1,3-GlcNAc-β1,4-Man) preceding matriglycan synthesis, is required for LARGE1-mediated generation of full-length matriglycan on α-DG (~150 kDa). In the absence of gene expression in mouse skeletal muscle, LARGE1 synthesizes a very short matriglycan resulting in a ~ 90 kDa α-DG which binds laminin but cannot prevent eccentric contraction-induced force loss or muscle pathology. Solution NMR spectroscopy studies demonstrate that LARGE1 directly interacts with core M3 and binds preferentially to the phosphorylated form. Collectively, our study demonstrates that phosphorylation of core M3 by POMK enables LARGE1 to elongate matriglycan on α-DG, thereby preventing muscular dystrophy.
Gene Expression Phosphorylation Protein Kinases - metabolism Protein Kinases - genetics Animals Dystroglycans - metabolism N-Acetylglucosaminyltransferases - genetics Male Mice Muscle, Skeletal - physiology N-Acetylglucosaminyltransferases - metabolism Mannose - chemistry

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