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Papers In Press, published online ahead of print April 24, 2002
Department of Biological Sciences, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8501
Corresponding Author: shirose{at}bio.titech.ac.jp
Ig-Hepta is a member of a new subfamily of the heptahelical receptors and has an unusually long N terminus extending toward the extracellular side of the plasma membrane. Pulse-chase experiments in 293T cells using antisera specifically recognizing its N- and C-terminal regions demonstrated that Ig-Hepta is core-glycosylated cotranslationally and proteolytically processed into a two-chain form in the endoplasmic reticulum, followed by maturation of oligosaccharide chains and dimerization. The cleavage occurs at two highly conserved sites: one in a ¡§SEA¡¨ module near the N terminus and the other in the stalk region preceding the first transmembrane span, generating ~20-kDa, 130-kDa, and 32-kDa fragments. The latter two remain tightly associated non-covalently even after cleavage as revealed by immunoprecipitation of native and myc-tagged Ig-Hepta constructs that were transiently expressed in 293T cells. The dimer consisting of four chains [(130 kDa + 32 kDa)2] is linked by disulfide bonds. A fusion protein of the extracellular domain of Ig-Hepta and the Fc domain of immunoglobulin was found to be a good substrate of the processing enzymes and used for determining the exact cleavage sites in the SEA module and juxtamembrane stalk region.
J. Biol. Chem, 10.1074/jbc.M110877200
Submitted on November 13, 2001
Revised on April 2, 2002
Accepted on April 23, 2002
Processing and subunit structure of Ig-Hepta, a seven-transmembrane receptor with a Long N-terminal extracellular domain
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