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Vol. 11, Issue 1, 65-77, January 2000
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*McGill Cancer Centre and Departments of Associations between plasma membrane-linked proteins and the actin
cytoskeleton play a crucial role in defining cell shape and
determination, ensuring cell motility and facilitating cell-cell or
cell-substratum adhesion. Here, we present evidence that CEACAM1-L, a
cell adhesion molecule of the carcinoembryonic antigen family, is
associated with the actin cytoskeleton. We have delineated the regions
involved in actin cytoskeleton association to the distal end of the
CEACAM1-L long cytoplasmic domain. We have demonstrated that CEACAM1-S,
an isoform of CEACAM1 with a truncated cytoplasmic domain, does not
interact with the actin cytoskeleton. In addition, a major difference
in subcellular localization of the two CEACAM1 isoforms was observed.
Furthermore, we have established that the localization of CEACAM1-L at
cell-cell boundaries is regulated by the Rho family of GTPases. The
retention of the protein at the sites of intercellular contacts
critically depends on homophilic CEACAM1-CEACAM1 interactions and
association with the actin cytoskeleton. Our results provide new
evidence on how the Rho family of GTPases can control cell adhesion: by
directing an adhesion molecule to its proper cellular destination. In
addition, these results provide an insight into the mechanisms of why
CEACAM1-L, but not CEACAM1-S, functions as a tumor cell growth inhibitor.
Anatomy and
Cell Biology and Biochemistry, Medicine, and Oncology,
McGill University, Montreal, Quebec, Canada H3G 1Y6
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