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J. Biol. Chem., Vol. 277, Issue 13, 11050-11057, March 29, 2002
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From the MAGP1 is a small molecular mass 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. This study identified a 54-amino acid sequence in the
carboxyl-terminal region of the protein that defines a matrix-binding
domain 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 contains a sequence similar to the matrix-binding domain 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), localized
intracellularly when expressed as chimeric proteins with green
fluorescent protein in rat lung fibroblasts. This suggests a second
action site for MAGP1.
Identification of a Matrix-binding Domain in MAGP1 and MAGP2 and
Intracellular Localization of Alternative Splice Forms*
,,,¶
Department of Cell Biology and Physiology
and the § Division of Pulmonary and Critical Care Medicine,
Department of Medicine, Barnes-Jewish Hospital and Washington
University School of Medicine, St. Louis, Missouri 63110
*
This work was supported by Grants HL53325, HL62295, and
HL61006 from the National Institutes of Health and by a grant from the
National Marfan Foundation.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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