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Beschreibung

Dystroglycan (UniProt: Q14118, also known as Dystrophin-associated glycoprotein 1) is encoded by the DAG1 gene (Gene ID: 1605) in human. The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. It also serves as an adhesion molecule and links the extracellular matrix to the intracellular actin cytoskeleton. Its expression is reported in a variety of fetal and adult tissues. It is synthesized with a signal peptide (aa 1-29) that is subsequently cleaved off to generate the mature protein that is further autolytically cleaved (between 653-654) to produce -dystroglycan (aa 30-653) and beta-dystroglycan (aa 654-895). -dystroglycan is an extracellular peripheral glycoprotein that binds to several extracellular matrix and synaptic proteins such as laminin-2 and 5, agrin, neurexin, and pikachurin. It is heavily O-glycosylated, which comprises of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. It is reported that its O-mannosyl glycosylation is required for its ligand- binding functions. It plays important roles in the deposition, organization, and stability of basement membranes. beta-dystroglycan is a single-pass type 1 transmembrane protein with its cytoplasmic tail bound to utrophin or dystrophin. It plays important roles in connecting the extracellular matrix to the cytoskeleton and serves as a cell adhesion receptor in both muscle and non-muscle tissues. In the cell, beta-dystroglycan binds to dystrophin that is linked to actin cytoskeleton. Hence, /beta- dystroglycans act as a molecular axis connecting extracellular matrix with the cytoskeleton across the plasma membrane. Defects in O-mannosyl glycan have been linked to various congenital muscular dystrophies caused by aberrant -dystroglycan glycosylation. (Ref.: Alonso-Rangel, L., et al. (2017). Life Sci. 182, 1-9, Yoon, JH., et al. (2012). J Proteome Res. 11(9), 4413-4424).