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Fig. 1. Several Drosophila ADAM metalloproteases cleave Delta and Serrate
in S2 cells. (A) Phylogenetic tree of ADAM metalloproteases.
Drosophila in bold, Anopheles in gray, C. elegans
in italics and human underlined. The different human ADAMs have distinct
homologs in each of the species. Note that ADAM10 has two homologs in
Drosophila (Kuz and Kul) and in Anopheles. Similarly,
Meltrin-
has two homologs in insects. (B) Kuz and Kul have all the
signature domains of ADAM metalloproteases. In the protease and disintegrin
domains, Kul shows a higher degree of similarity to the human ADAM10. (C) Dl
or Ser were expressed in S2 cells, and their capacity to serve as substrates
for co-expressed Drosophila ADAM metalloproteases monitored by the
appearance of ligand in the medium, and the concomitant disappearance from the
cells. Kul, Kuz and DTACE displayed potent cleavage of both ligands. DMeltrin
induced only low levels of Ser cleavage. The activity of the Mmd Meltrin
homolog was not examined, because its expression is restricted to the central
nervous system (Chase et al.,
1987).
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