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TitleLARGE1 processively polymerizes length-controlled matriglycan on prodystroglycan.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9028, Year 2025
Publish dateOct 10, 2025
AuthorsSoumya Joseph / Nicholas J Schnicker / Nicholas Spellmon / Zhen Xu / Rui Yan / Zhiheng Yu / Omar Davulcu / Tiandi Yang / Jesse Hopkins / Mary E Anderson / David Venzke / Kevin P Campbell /
PubMed AbstractMatriglycan is a linear glycan (xylose-β1,3-glucuronate), which binds proteins in the extracellular matrix that contain laminin-globular domains and Lassa Fever Virus. It is indispensable for ...Matriglycan is a linear glycan (xylose-β1,3-glucuronate), which binds proteins in the extracellular matrix that contain laminin-globular domains and Lassa Fever Virus. It is indispensable for neuromuscular function. Matriglycan of insufficient length can cause muscular dystrophy with abnormal brain and eye development. LARGE1 (Like-acetylglucosaminyltransferase-1) uniquely synthesizes matriglycan on dystroglycan. The mechanism of matriglycan synthesis is not obvious from cryo-EM reconstructions of LARGE1. However, by reconstituting activity in vitro on recombinant prodystroglycan we show that the presence of the dystroglycan N-terminal domain (DGN), phosphorylated core M3, and a xylose-glucuronate primer are necessary for matriglycan polymerization by LARGE1. By introducing active site mutations, we demonstrate that LARGE1 processively polymerizes matriglycan on prodystroglycan, with its length regulated by the dystroglycan prodomain, DGN. Our enzymatic analysis of LARGE1 uncovers the mechanism of matriglycan synthesis on dystroglycan, which can form the basis for therapeutic strategies to treat matriglycan-deficient neuromuscular disorders and arenaviral infections.
External linksNat Commun / PubMed:41073435 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

47420

9e1t

EMDB-47420: CryoEM structure of LARGE1 bound to UDP
PDB-9e1t: CryoEM structure of LARGE1 bound to UDP-GlcA
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-UGA:
URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Glycosyltransferase

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