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The receptor-like protein tyrosine phosphatases (RPTP) µ and
RPTP
Volume 270,
Number 24,
Issue of June 16, pp. 14247-14250, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and
A CRITICAL ROLE FOR THE NOVEL EXTRACELLULAR MAM DOMAIN
have a modular ectodomain consisting of four fibronectin type
III-like repeats, a single Ig-like domain, and a newly identified
N-terminal MAM domain. The function of the latter module, which
comprises about 160 amino acids and is found in diverse transmembrane
proteins, is not known. We previously reported that both RPTPµ and
RPTP can mediate homophilic cell interactions when expressed in
insect cells. Here we show that despite their striking structural
similarity, RPTPµ and RPTP fail to interact in a heterophilic
manner. To examine the role of the MAM domain in homophilic binding, we
expressed a mutant RPTPµ lacking the MAM domain in insect Sf9
cells. Truncated RPTPµ is properly expressed at the cell surface
but fails to promote cell-cell adhesion. Homophilic cell adhesion is
fully restored in a chimeric RPTPµ molecule containing the MAM
domain of RPTP. However, this chimeric RPTPµ does not interact
with either RPTPµ or RPTP. These results indicate that the MAM
domain of RPTPµ and RPTP is essential for homophilic cell-cell
interaction and helps determine the specificity of these interactions.
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