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J. Biol. Chem., Vol. 277, Issue 26, 23391-23398, June 28, 2002
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From the Department of Biological Sciences, Tokyo Institute of
Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan
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 (a module first
identified in sperm protein, enterokinase, and
agrin) near the N terminus and the other in the stalk
region preceding the first transmembrane span, generating ~20-, 130-, 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.
Cleavage of Ig-Hepta at a "SEA" Module and at a Conserved G
Protein-coupled Receptor Proteolytic Site*
*
This work was supported by grant-in-aid for Scientific
Research 0910200 from the Ministry of Education, Culture, Sport,
Science and Technology of Japan, by Research Grant for Cardiovascular Diseases 11C-1 from the Ministry of Health, Labour and Welfare of
Japan, and by an SRF Grant for Biomedical Research.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.
To whom correspondence should be addressed. Tel.: 81-45-924-5726;
Fax: 81-45-924-5824; E-mail: shirose@bio.titech.ac.jp.
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