Overview:

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 (1). 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 (2).

References:

1. Hoodless, P. A. et al: MADR1, a MAD-related protein that functions in BMP2 signaling pathways. Cell 85: 489-500, 1996.2. Nakashima, K. et al: Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. Science 284: 479-482, 1999.