Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of α-dystroglycan

Renzhi Han, Motoi Kanagawa, Takako Yoshida-Moriguchi, Erik P. Rader, Rainer A. Ng, Daniel E. Michele, David E. Muirhead, Stefan Kunz, Steven A. Moore, Susan T. Iannaccone, Katsuya Miyake, Paul L. McNeil, Ulrike Mayer, Michael B A Oldstoned, John A. Faulkner, Kevin P. Campbell

Research output: Contribution to journalArticlepeer-review

120 Scopus citations


Skeletal muscle basal lamina is linked to the sarcolemma through transmembrane receptors, including integrins and dystroglycan. The function of dystroglycan relies critically on posttranslational glycosylation, a common target shared by a genetically heterogeneous group of muscular dystrophies characterized by α-dystroglycan hypoglycosylation. Here we show that both dystroglycan and integrin α7 contribute to force-production of muscles, but that only disruption of dystroglycan causes detachment of the basal lamina from the sarcolemma and renders muscle prone to contraction-induced injury. These phenotypes of dystroglycan-null muscles are recapitulated by Large myd muscles, which have an intact dystrophin-glycoprotein complex and lack only the laminin globular domain-binding motif on α-dystroglycan. Compromised sarcolemmal integrity is directly shown in Largemyd muscles and similarly in normal muscles when arenaviruses compete with matrix proteins for binding α-dystroglycan. These data provide direct mechanistic insight into how the dystroglycan-linked basal lamina contributes to the maintenance of sarcolemmal integrity and protects muscles from damage.

Original languageEnglish (US)
Pages (from-to)12573-12579
Number of pages7
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number31
StatePublished - Aug 4 2009


  • Dystroglycanopathy
  • Glycosylation
  • Integrin
  • Membrane damage
  • Muscular dystrophy

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Basal lamina strengthens cell membrane integrity via the laminin G domain-binding motif of α-dystroglycan'. Together they form a unique fingerprint.

Cite this