SMAD1 is a member of the SMAD family which are signal transducers and transcriptional modulators that mediate multiple signaling pathways. The actions of bone morphogenetic proteins (BMPs) are mediated by SMAD1 and SMAD1 can be phosphorylated and activated by the BMP receptor kinase. Phosphorylated SMAD1 forms a complex with SMAD4 that is important for its function in the transcription regulation. The SMAD1-SMAD4 complex is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. The formation of a complex between STAT3 and SMAD1, bridged by p300, is involved in the cooperative signaling of LIF and BMP2 and the subsequent induction of astrocytes from neuronal progenitors.
Components of the signaling pathways that lie downstream of Ser/Thr kinase receptors and are required for signaling by the TGF beta superfamily have been poorly defined. The Drosophila gene Mothers against dpp (MAD) and the C. elegans sma genes are
Science (New York, N.Y.), 284(5413), 479-482 (1999-04-16)
The cytokines LIF (leukemia inhibitory factor) and BMP2 (bone morphogenetic protein-2) signal through different receptors and transcription factors, namely STATs (signal transducers and activators of transcription) and Smads. LIF and BMP2 were found to act in synergy on primary fetal
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