Fukutin-Related Protein Associates with the Sarcolemmal Dystrophin
Supplemental Material can be found at: http://www.jbc.org/cgi/content/full/C700061200/DC1 ACCELERATED PUBLICATION This paper is available online at www.jbc.org THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 282, NO. 23, pp. 16713–16717, June 8, 2007 © 2007 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. Fukutin-related Protein with variable heart, respiratory, and brain involvement (1–3). Although the specific function of FKRP is unclear, FKRP and its Associates with the closest known homolog fukutin share sequence homology with Sarcolemmal Dystrophin- phosphoryl ligand transferases and contain DXD domains common to some glycosyltransferases (4, 5). In addition, FKRP- *□S Glycoprotein Complex associated muscular dystrophies fall into a growing family of Received for publication, March 30, 2007, and in revised form, April 17, 2007 “dystroglycanopathies,” which exhibit reduced glycosylation of Published, JBC Papers in Press, April 23, 2007, DOI 10.1074/jbc.C700061200 membrane-associated ␣DG (6). Extracellular ␣DG and the 1 2 Aaron M. Beedle , Patricia M. Nienaber, and Kevin P. Campbell transmembrane-spanning DG bind to dystrophin, sarcogly- From the Howard Hughes Medical Institute (HHMI) and the Departments cans, and other proteins to form the dystrophin-glycoprotein of Molecular Physiology and Biophysics, Internal Medicine, and Neurology, University of Iowa Carver College of Medicine, Iowa City, Iowa 52242 complex (DGC), which serves as a critical structural link between the cell cytoskeleton, the sarcolemma, and the extra- Mutations in fukutin-related protein (FKRP) give rise to mild cellular basement membrane. ␣DG glycans, detected by anti- Downloaded from and more severe forms of muscular dystrophy.
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