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Papers In Press, published online ahead of print January 16, 2002
Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110
Corresponding Author: bmecham{at}cellbiology.wustl.edu
Microfibril-associated glycoprotein-1 (MAGP1) is a small molecular weight protein associated with microfibrils in the extracellular matrix (ECM). To identify the molecular basis of its interaction with other microfibrillar proteins, deletion constructs of MAGP1 were expressed in a mammalian cell system that served as a model for microfibril assembly. These studies identified a 54 amino acid sequence in the carboxy-terminal region of the protein that defines a matrix-binding domain (MBD) that is sufficient to target MAGP1 to the ECM. Site-directed mutagenesis demonstrated that binding activity is dependent on the presence of 7 cysteine residues in this sequence. MAGP2 contained a sequence similar to the MBD of MAGP1 but could not associate with the ECM because of a single amino acid change. Two naturally occurring MAGP1 splice variants, MAGP1B (human specific) and Magp1D (found in mice), localize intracellularly when expressed as chimeric proteins with the green fluorescent protein in rat lung fibroblasts. This suggests a second action site for MAGP1.
J. Biol. Chem, 10.1074/jbc.M110347200
Submitted on October 28, 2001
Revised on January 14, 2002
Accepted on January 15, 2002
Identification of a matrix binding domain in the microfibril-associated glycoproteins 1 and 2 (MAGP1 and 2) and cellular localization of alternative splice forms
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