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J. Cell Biol.,
Volume 142, Number 1, July 13, 1998 251-261
* University of Michigan, Department of Anatomy and Cell Biology, Ann Arbor, Michigan 48109-0616; and Expression of the Drosophila cell adhesion
molecule neuroglian in S2 cells leads to cell aggregation
and the intracellular recruitment of ankyrin to cell contact sites. We localized the region of neuroglian that interacts with ankyrin and investigated the mechanism
that limits this interaction to cell contact sites. Yeast
two-hybrid analysis and expression of neuroglian deletion constructs in S2 cells identified a conserved 36-amino acid sequence that is required for ankyrin binding. Mutation of a conserved tyrosine residue within
this region reduced ankyrin binding and extracellular
adhesion. However, residual recruitment of ankyrin by
this mutant neuroglian molecule was still limited to cell
contacts, indicating that the lack of ankyrin binding at
noncontact sites is not caused by tyrosine phosphorylation. A chimeric molecule, in which the extracellular
domain of neuroglian was replaced with the corresponding domain from the adhesion molecule fasciclin II, also selectively recruited ankyrin to cell contacts.
Thus, outside-in signaling by neuroglian in S2 cells depends on extracellular adhesion, but does not depend
on any unique property of its extracellular domain. We
propose that the recruitment of ankyrin to cell contact sites depends on a physical rearrangement of neuroglian in response to cell adhesion, and that ankyrin
binding plays a reciprocal role in stabilizing the adhesive interaction.
University of
Chicago, Department of Pharmacological and Physiological Sciences, Chicago, Illinois 60637
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