Utrophin-dystroglycan complex in membranes of adherent cultured cells

Marian James, Nguyen Thi Man, Clare J. Wise, Gareth E. Jones, Glenn E. Morris*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)

Abstract

In skeletal muscle, dystrophin binds to an oligomeric, transmembrane complex (DAGc; dystrophin-associated glycoprotein complex) which interacts with laminin in the extracellular matrix. We now present biochemical evidence for an association between utrophin (dystrophin-related protein, DRP) and a major DAGc component, β-dystroglycan (43DAG) in cultured cell lines which contain little if any dystrophin. We have shown also that utrophin and β- dystroglycan co-localise at or near the plasma membrane and that they co- sediment in large complexes on sucrose density gradients. On the lower plasma membrane, in contact with the substratum, part of the utrophin and β- dystroglycan staining co-localised with α-actinin in a punctate distribution outside classical vinculin-rich focal adhesions. β-dystroglycan, utrophin, syntrophin (59DAP), and α-actinin were found in all adhesion competent cell lines studied, but levels of the last three proteins were greatly reduced in myeloma cells, which cannot readily attach to substrata. Possible roles for utrophin in cultured cells are considered in the light of recent evidence for involvement of utrophin-glycoprotein complexes in muscle in signal transduction and recruitment of acetylcholine receptors to neuromuscular junctions.

Original languageEnglish
Pages (from-to)163-174
Number of pages12
JournalCell Motility and the Cytoskeleton
Volume33
Issue number3
DOIs
Publication statusPublished - 22 Apr 1996

Keywords

  • actin cytoskeleton
  • actinin
  • cell adhesion
  • dystrophin-related protein (DRP)
  • muscular dystrophy
  • syntrophin

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