Disruption of perlecan binding and matrix assembly by post-translational or genetic disruption of dystroglycan function

Motoi Kanagawa; Daniel E Michele; Jakob S Satz; Rita Barresi; Hajime Kusano; Takako Sasaki; Rupert Timpl; Michael D Henry; Kevin P Campbell

doi:10.1016/j.febslet.2005.07.059

Back

Disruption of perlecan binding and matrix assembly by post-translational or genetic disruption of dystroglycan function

Journal article

Peer reviewed

Disruption of perlecan binding and matrix assembly by post-translational or genetic disruption of dystroglycan function

Motoi Kanagawa, Daniel E Michele, Jakob S Satz, Rita Barresi, Hajime Kusano, Takako Sasaki, Rupert Timpl, Michael D Henry and Kevin P Campbell

FEBS letters, Vol.579(21), pp.4792-4796

2005

DOI: 10.1016/j.febslet.2005.07.059

PMID: 16098969

View Online

Abstract

Dystroglycan is a cell-surface matrix receptor that requires LARGE-dependent glycosylation for laminin binding. Although the interaction of dystroglycan with laminin has been well characterized, less is known about the role of dystroglycan glycosylation in the binding and assembly of perlecan. We report reduced perlecan-binding activity and mislocalization of perlecan in the LARGE-deficient Large myd mouse. Cell-surface ligand clustering assays show that laminin polymerization promotes perlecan assembly. Solid-phase binding assays provide evidence for the first time of a trimolecular complex formation of dystroglycan, laminin and perlecan. These data suggest functional disruption of the trimolecular complex in glycosylation-deficient muscular dystrophy.

Dystroglycan

Laminin

Congenital muscular dystrophy

Perlecan

Basement membrane

Large myd mouse

Details

Title: Subtitle: Disruption of perlecan binding and matrix assembly by post-translational or genetic disruption of dystroglycan function
Creators: Motoi Kanagawa - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Daniel E Michele - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Jakob S Satz - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Rita Barresi - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Hajime Kusano - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Takako Sasaki - Max-Planck-Institut fur Biochemie, Martinsried D-82152, Germany
Rupert Timpl - Max-Planck-Institut fur Biochemie, Martinsried D-82152, Germany
Michael D Henry - Department of Physiology and Biophysics, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, Iowa City, IA 52242, USA
Kevin P Campbell - Department of Physiology and Biophysics, Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa, 400 Eckstein Medical Building, Iowa City, IA 52242, USA
Resource Type: Journal article
Publication Details: FEBS letters, Vol.579(21), pp.4792-4796
DOI: 10.1016/j.febslet.2005.07.059
PMID: 16098969
NLM abbreviation: FEBS Lett
ISSN: 0014-5793
eISSN: 1873-3468
Publisher: Elsevier B.V
Language: English
Date published: 2005
Academic Unit: Neurology; Molecular Physiology and Biophysics; Pathology; Iowa Neuroscience Institute; Radiation Oncology; Urology
Record Identifier: 9984020847902771

Metrics

17 Record Views

49 Times Cited - Web of Science