Upon phosphorylation by type I receptors, receptor-regulated Smads (R-Smads; Smad2 and 3) form heteromeric complexes with common-partner Smad (Co-Smad; Smad4) and translocate into the nucleus.
Class II NRs bind to HREs with direct repeats (DRs) and heterodimerize with the common partner, RXR.
Despite use for over 100 years, it wasn't until 2007 that we discovered that Yellow #5 (tartrazine) had been reacting dangerously with a common partner preservative.
Altered interactions with a common partner such as LPrP [35] deriving from selection for an altered form of PrP might in turn select for a compensatory allelic form of Sho.
The combined use of biochemical and biophysical approaches indicated that this functional cooperation relies on the alternate association of these receptors with a common partner, endogenously expressed in our cell system.
Two of any activated R-Smad proteins form a heterotrimer with a common partner, Smad4.
This phosphorylation event allows for subsequent heterotrimerization of two phosphorylated R-Smad subunits with one common partner, Smad4 [ 13, 14].
These associate with the common partner Smad 4 (Co-Smad 4), creating a complex which translocates to the nucleus to facilitate target gene transcription.
The activated type I receptor phosphorylates specific receptor-regulated Smad proteins, which then form a complex with the common partner Smad4 (Piek et al, 1999).
