POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan

POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan

Matriglycan [-GlcA-β1,3-Xyl-α1,3-]n 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...

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Bibliographic Details
Main Authors: Ameya S Walimbe, Hidehiko Okuma, Soumya Joseph, Tiandi Yang, Takahiro Yonekawa, Jeffrey M Hord, David Venzke, Mary E Anderson, Silvia Torelli, Adnan Manzur, Megan Devereaux, Marco Cuellar, Sally Prouty, Saul Ocampo Landa, Liping Yu, Junyu Xiao, Jack E Dixon, Francesco Muntoni, Kevin P Campbell
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2020-09-01
Series:eLife
Subjects:
dystroglycan
matriglycan
LARGE
POMK
laminin
muscular dystrophy
Online Access:https://elifesciences.org/articles/61388

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