High degree of conservation of the enzymes synthesizing the laminin-binding glycoepitope of α-dystroglycan

Maria Giulia Bigotti*, Andrea Brancaccio*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

4 Citations (Scopus)
57 Downloads (Pure)


The dystroglycan (DG) complex plays a pivotal role for the stabilization of muscles in Metazoa. It is formed by two subunits, extracellular α-DG and transmembrane β-DG, originating from a unique precursor via a complex post-translational maturation process. The α-DG subunit is extensively glycosylated in sequential steps by several specific enzymes and employs such glycan scaffold to tightly bind basement membrane molecules. Mutations of several of these enzymes cause an alteration of the carbohydrate structure of α-DG, resulting in severe neuromuscular disorders collectively named dystroglycanopathies. Given the fundamental role played by DG in muscle stability, it is biochemically and clinically relevant to investigate these post-translational modifying enzymes from an evolutionary perspective. A first phylogenetic history of the thirteen enzymes involved in the fabrication of the so-called ‘M3 core’ laminin-binding epitope has been traced by an overall sequence comparison approach, and interesting details on the primordial enzyme set have emerged, as well as substantial conservation in Metazoa. The optimization along with the evolution of a well-conserved enzymatic set responsible for the glycosylation of α-DG indicate the importance of the glycosylation shell in modulating the connection between sarcolemma and surrounding basement membranes to increase skeletal muscle stability, and eventually support movement and locomotion.
Original languageEnglish
Article number210104
Pages (from-to)210104
Number of pages1
JournalOpen Biology
Issue number9
Publication statusPublished - 29 Sept 2021

Bibliographical note

Funding Information:
M.G.B. is funded by the British Heart Foundation (grant no. CH/1/32804).

Publisher Copyright:
© 2021 The Authors.


  • glycosyltransferases
  • post-translational glycosylation
  • M3 core structure
  • e, laminin-binding glycoepitope
  • protein evolution


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