Biochemical Journal

Research article

Direct interaction of β-dystroglycan with F-actin

Yun-Ju CHEN, Heather J. SPENCE, Jacqueline M. CAMERON, Thomas JESS, Jane L. ILSLEY, Steven J. WINDER


Dystroglycans are essential transmembrane adhesion receptors for laminin. α-Dystroglycan is a highly glycosylated extracellular protein that interacts with laminin in the extracellular matrix and the transmembrane region of β-dystroglycan. β-Dystroglycan, via its cytoplasmic tail, interacts with dystrophin and utrophin and also with the actin cytoskeleton. As a part of the dystrophin–glycoprotein complex of muscles, dystroglycan is also important in maintaining sarcolemmal integrity. Mutations in dystrophin that lead to Duchenne muscular dystrophy also lead to a loss of dystroglycan from the sarcolemma, and chimaeric mice lacking muscle dystroglycan exhibit a severe muscular dystrophy phenotype. Using yeast two-hybrid analysis and biochemical and cell biological studies, we show, in the present study, that the cytoplasmic tail of β-dystroglycan interacts directly with F-actin and, furthermore, that it bundles actin filaments and induces an aberrant actin phenotype when overexpressed in cells.

  • actin binding
  • actin bundling
  • dystroglycan
  • F-actin
  • muscular dystrophy
  • utrophin


  • Abbreviations used: α/β-DG, full-length dystroglycan; AP, alkaline phosphatase; DG, dystroglycan; DGC, dystrophin–glycoprotein complex; DGc, cytoplasmic domain of β-DG; DGe, extracellular domain of β-DG; GFP, green fluorescent protein; GST, glutathione S-transferase; PAK, p21-activated kinase.