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

ABSTRACT: 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 persp

SUBMITTER: Bigotti MG 

PROVIDER: S-EPMC8478517 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature