XB-ART-1376Biochem J January 1, 2006; 393 (Pt 1): 311-20.
In a search for binding partners to Smad8, we identified the chicken homologue of the mammalian Tid1 protein (cTid1), which is a regulator of apoptosis related to the Drosophila tumour suppressor Tid56. The cTid1 coding sequence is highly conserved with mammalian Tid1, including the DnaJ domain that interacts with Hsp70 (heat-shock protein 70). The cTid1 gene is widely expressed with transcripts enriched in the developing blood islands of the embryonic-yolk sac. We show that cTid1 can bind to other members of the Smad family and that highest binding activity occurs with the negative regulatory Smad7, through the conserved MH2 domain. This interaction can have functional relevance in vivo, since co-expression of Tid1 blocks the dorsalizing and BMP (bone morphogenetic protein)-dependent regulatory activity of Smad7 in developing Xenopus embryos. The finding that these proteins can interact suggests the potential for linking two important cell survival/apoptosis pathways.
PubMed ID: 16156721
PMC ID: PMC1383690
Article link: Biochem J
Species referenced: Xenopus laevis
Genes referenced: dnaja2 dnaja3 hsp70 hspa1l smad7
References [+] :
Canamasas, Understanding human cancer using Drosophila: Tid47, a cytosolic product of the DnaJ-like tumor suppressor gene l2Tid, is a novel molecular partner of patched related to skin cancer. 2003, Pubmed