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

125 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


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