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Vol. 9, Issue 8, 2145-2156, August 1998
*Department of Biochemistry, The Cancer Institute, Japanese
Foundation for Cancer Research, and Research for the Future Program,
Japan Society for the Promotion of Science, Tokyo 170-8455, Japan;
Decapentaplegic (Dpp) plays an essential role in
Drosophila development, and analyses of the Dpp
signaling pathway have contributed greatly to understanding of the
actions of the TGF-Third Department of Internal Medicine, Yamaguchi
University School of Medicine, Yamaguchi 755-8505, Japan; and
Institute of Molecular and Cellular Biosciences,
University of Tokyo, Tokyo 113-0032, Japan
superfamily. Intracellular signaling of the
TGF- superfamily is mediated by Smad proteins, which are now grouped
into three classes. Two Smads have been identified in
Drosophila. Mothers against dpp (Mad) is a
pathway-specific Smad, whereas Daughters against dpp (Dad) is an
inhibitory Smad genetically shown to antagonize Dpp signaling. Here we
report the identification of a common mediator Smad in Drosophila, which is closely related to human Smad4. Mad
forms a heteromeric complex with Drosophila Smad4
(Medea) upon phosphorylation by Thick veins (Tkv), a type I receptor
for Dpp. Dad stably associates with Tkv and thereby inhibits
Tkv-induced Mad phosphorylation. Dad also blocks hetero-oligomerization
and nuclear translocation of Mad. We also show that Mad exists as a
monomer in the absence of Tkv stimulation. Tkv induces
homo-oligomerization of Mad, and Dad inhibits this step. Finally, we
propose a model for Dpp signaling by Drosophila Smad
proteins.
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