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J. Biol. Chem., Vol. 277, Issue 22, 19600-19608, May 31, 2002
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From the Department of Biochemistry, Faculty of Medicine, Kagoshima
University, Kagoshima 890-8520, Japan
Cadherins are transmembrane glycoproteins involved in
Ca2+-dependent cell-cell adhesion. Using
L cells coexpressing E-cadherin constructs with different epitope tags,
we examined the lateral dimerization of E-cadherin and its adhesive
activity by co-immunoprecipitation and aggregation assays,
respectively. Although the transmembrane domain is required for
dimerization, tail-less constructs possessing the transmembrane domain
of either N-cadherin or CD45 show dimerization and are active in
aggregation assays. Two mutant constructs having either of two amino
acid substitutions, W2A or substitutions that disrupt the recognition
sequence for endoproteolytic enzymes involved in removal of the
precursor segment, cannot form dimers and are inactive in aggregation.
These monomeric proteins, like their wild-type dimerizing counterparts,
retain their Ca2+-dependent resistance to
trypsin digestion, suggesting that dimerization per se does
not induce a large conformational change. Two other constructs, having
either an amino acid substitution, D134A, or a C-terminal deletion of
70 amino acid residues, retain the ability to associate laterally but
are inactive in aggregation assays. Staurosporine treatment of cells
expressing the latter construct increases aggregation but does
not increase the extent of lateral dimerization. Thus, lateral
dimerization is necessary, but not sufficient for adhesive activity.
Lateral Dimerization of the E-cadherin Extracellular Domain Is
Necessary but Not Sufficient for Adhesive Activity*
*
This work was supported by a grant-in-aid for science
research on priority area (B) from the Ministry of Education, Culture, Sports, Science and Technology of Japan.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 all correspondence should be addressed. Tel.:
81-99-275-5246; Fax: 81-99-264-5618; E-mail:
mozawa@m.kufm.kagoshima-u.ac.jp.
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