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(Received for publication, June 19, 1996, and in revised form, August 19, 1996)
From The Burnham Institute, La Jolla Cancer Research Center,
La Jolla, California 92307
To test whether glycosyl
phosphatidylinositol-linked T-cadherin is a component of cell junctions
like classical cadherins, we have examined its distribution and
targeting in polarized epithelial cells. In vivo,
T-cadherin was detected on the apical cell surface of the chick
intestinal epithelium. In cultures of transfected Madin-Darby canine
kidney cells, T-cadherin was also expressed apically, whereas classical
N-cadherin resided basolaterally. Both cadherins were directly targeted
to their respective membrane domains. Mutant proteins were expressed in
Madin-Darby canine kidney cells to identify the regions responsible for
differential cadherin localization. N
Volume 271, Number 47,
Issue of November 22, 1996
pp. 30061-30067
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
cyt, an N-cadherin cytoplasmic
domain deletion mutant, was stably distributed basolaterally. This
mutant was transported to both the apical and basolateral membrane
compartments, followed by preferential removal from the apical surface.
T-N
cyt, a T-cadherin mutant with the N-cadherin cytoplasmic domain
deletion, was localized basolaterally, whereas N-TGPI, a
GPI-anchored N-cadherin mutant, resided at the apical domain. The
T-cadherin carboxyl-terminal 76 amino acids contain the apical
targeting signal and include the signal for GPI anchor attachment.
Basolateral localization of N-cadherin is achieved through targeting
signals in the cytoplasmic domain. Thus, GPI-linked T-cadherin is not a
component of cell junctions, consistent with a function as a
recognition rather than a cell adhesion molecule.
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