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Vol. 9, Issue 7, 1709-1723, July 1998
Department of Biology, Indiana University, Bloomington, Indiana
47405
Delta functions as a cell nonautonomous membrane-bound ligand that
binds to Notch, a cell-autonomous receptor, during cell fate
specification. Interaction between Delta and Notch leads to signal
transduction and elicitation of cellular responses. During our
investigations to further understand the biochemical mechanism by which
Delta signaling is regulated, we have identified four Delta isoforms in
Drosophila embryonic and larval extracts. We have
demonstrated that at least one of the smaller isoforms, Delta S,
results from proteolysis. Using antibodies to the Delta extracellular
and intracellular domains in colocalization experiments, we have found
that at least three Delta isoforms exist in vivo, providing the first
evidence that multiple forms of Delta exist during development.
Finally, we demonstrate that Delta is a transmembrane ligand that can
be taken up by Notch-expressing Drosophila cultured cells. Cell culture experiments imply that full-length Delta is taken
up by Notch-expressing cells. We present evidence that suggests this
uptake occurs by a nonphagocytic mechanism.
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