The complexities of dystroglycan

Trends Biochem Sci. 2001 Feb;26(2):118-24. doi: 10.1016/s0968-0004(00)01731-x.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Division
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / physiology*
  • Cytoskeleton / metabolism
  • Dystroglycans
  • Laminin / chemistry
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / physiology*
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Tertiary
  • Signal Transduction


  • Cytoskeletal Proteins
  • Laminin
  • Membrane Glycoproteins
  • Dystroglycans