Dystroglycan versatility in cell adhesion: a tale of multiple motifs

Cell Communication and Signaling

Review

Steve J Winder¹  Chris J Moore¹ 

[1] Department of Biomedical Science, University of Sheffield, Firth Court, Western Bank, S10 2TN, Sheffield, UK;

关键词: Duchenne Muscular Dystrophy;    Congenital Muscular Dystrophy;    Filopodium Formation;    Dystrophin Glycoprotein Complex;    Juxtamembrane Region;   

DOI  :  10.1186/1478-811X-8-3

 received in 2009-12-29, accepted in 2010-02-17,  发布年份 2010

来源: Springer

【 摘 要 】

Dystroglycan is a ubiquitously expressed heterodimeric adhesion receptor. The extracellular α-subunit makes connections with a number of laminin G domain ligands including laminins, agrin and perlecan in the extracellular matrix and the transmembrane β-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 spatio-temporal regulation.

【 授权许可】

CC BY   
© Moore and Winder; licensee BioMed Central Ltd. 2010