TY - JOUR
T1 - Identification of a novel Drosophila SMAD on the X chromosome
AU - Henderson, Katya D.
AU - Andrew, Deborah J.
N1 - Funding Information:
We thank D. Barrick and P. Bradley for their critical comments on this manuscript. We are grateful for the fly stocks that were provided by the Indiana and Umea Stock Centers, and A. Christensen. We thank the Berkeley Drosophila Genome Project for their progress and for the ease with which their databases are accessed and desired clones provided. Sequencing was done by the Johns Hopkins University School of Medicine Genetics Core DNA Analysis Facility. We thank C. Machado for providing a developmental Northern and all the members of the Andrew laboratory for their help throughout this work. This work was supported by NIH grant # R01 GM51311.
PY - 1998/11/9
Y1 - 1998/11/9
N2 - TGF-β signaling from the cell surface to the nucleus is mediated by the SMAD family of proteins, which have been grouped into three classes based upon sequence identity and function. Receptor-regulated, or pathway-restricted, SMADs (R-SMADs) are phosphorylated by ligand-specific serine/threonine kinase receptors. Phosphorylated R-SMADs oligomerize with the coactivating, or shared, SMAD (Co-SMAD) mediator and translocate to the nucleus where the complex directs transcription of downstream target genes. Inhibitory SMADs (I-SMADs) block receptor-mediated phosphorylation of R-SMADs. In Drosophila, one member of each class of SMAD has been reported: MAD, an R-SMAD, MEDEA, a Co-SMAD, and DAD, an I-SMAD. Here, we report the first identification of a novel Drosophila R-SMAD, which we have named Smox for Smad on X. We have localized the Smox gene to a specific interval on the X chromosome and shown that Smox is transcribed throughout development.
AB - TGF-β signaling from the cell surface to the nucleus is mediated by the SMAD family of proteins, which have been grouped into three classes based upon sequence identity and function. Receptor-regulated, or pathway-restricted, SMADs (R-SMADs) are phosphorylated by ligand-specific serine/threonine kinase receptors. Phosphorylated R-SMADs oligomerize with the coactivating, or shared, SMAD (Co-SMAD) mediator and translocate to the nucleus where the complex directs transcription of downstream target genes. Inhibitory SMADs (I-SMADs) block receptor-mediated phosphorylation of R-SMADs. In Drosophila, one member of each class of SMAD has been reported: MAD, an R-SMAD, MEDEA, a Co-SMAD, and DAD, an I-SMAD. Here, we report the first identification of a novel Drosophila R-SMAD, which we have named Smox for Smad on X. We have localized the Smox gene to a specific interval on the X chromosome and shown that Smox is transcribed throughout development.
KW - ACTIVIN
KW - DPP
KW - Drosophila
KW - SMADs
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U2 - 10.1006/bbrc.1998.9562
DO - 10.1006/bbrc.1998.9562
M3 - Article
C2 - 9813169
AN - SCOPUS:0032501157
SN - 0006-291X
VL - 252
SP - 195
EP - 201
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -