1 research outputs found
Dystroglycan versatility in cell adhesion: a tale of multiple motifs
Dystroglycan is a ubiquitously expressed heterodimeric adhesion receptor. The extracellular a-subunit makes connections
with a number of laminin G domain ligands including laminins, agrin and perlecan in the extracellular
matrix and the transmembrane b-subunit makes connections to the actin filament network via cytoskeletal linkers
including dystrophin, utrophin, ezrin and plectin, depending on context. Originally discovered as part of the dystrophin
glycoprotein complex of skeletal muscle, dystroglycan is an important adhesion molecule and signalling scaffold
in a multitude of cell types and tissues and is involved in several diseases. Dystroglycan has emerged as a
multifunctional adhesion platform with many interacting partners associating with its short unstructured cytoplasmic
domain. Two particular hotspots are the cytoplasmic juxtamembrane region and at the very carboxy terminus
of dystroglycan. Regions which between them have several overlapping functions: in the juxtamembrane region; a
nuclear localisation signal, ezrin/radixin/moesin protein, rapsyn and ERK MAP Kinase binding function, and at the C
terminus a regulatory tyrosine governing WW, SH2 and SH3 domain interactions. We will discuss the binding partners
for these motifs and how their interactions and regulation can modulate the involvement of dystroglycan in a
range of different adhesion structures and functions depending on context. Thus dystroglycan presents as a multifunctional
scaffold involved in adhesion and adhesion-mediated signalling with its functions under exquisite spatiotemporal
regulation