The complexities of dystroglycan.
The notion of dystroglycan as a simple laminin-binding receptor is increasingly being challenged. New roles and new binding partners are continually emerging. Recent structural advances have provided exciting new insights into the precise molecular interactions between dystroglycan and other key components of the dystroglycan complex. Coupled with an increasing understanding of dystroglycan function at the molecular level, we are finally beginning to probe the complexities of dystroglycan, not only in disease, but in development, adhesion and signalling.
Winder
S J
SJ
Institute of Biomedical and Life Sciences, Division of Biochemistry and Molecular Biology, Davidson Building, University of Glasgow, G12 8QQ, Glasgow, UK. s.winder@bio.gla.ac.uk
D000818:Animals; D002448:Cell Adhesion; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000502:physiology*; D003599:Cytoskeleton / Q000378:metabolism; D049030:Dystroglycans; D007797:Laminin / Q000737:chemistry; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000502:physiology*; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
D003598:Cytoskeletal Proteins; D007797:Laminin; D008562:Membrane Glycoproteins; D049030:Dystroglycans