When glucose uptake or a shift from glycolysis to oxidative phosphorylation is blocked, the transcriptional activities of YAP/TAZ are decreased via modulating the complex formation between TEADs and YAP/TAZ (Enzo et al., 2015).
However, how the complex formation is regulated is unclear.
SCF dimer mediates the complex formation of KIT extracellular domains.
The complex formation is fast and efficient.
To obtain mechanistic insights into how acetylation of Sox2 and Oct4 modulate their complex formation, we tried to pinpoint the acetylation sites on both Sox2 and Oct4.
From a more general viewpoint, this study shows that the oligosaccharides displayed on proteins can modulate complex formation, positively and negatively, not only through intermolecular carbohydrate protein and carbohydrate carbohydrate interactions but also by influencing protein dynamics coupled with the selection of protein protein interaction modes.
Many of the known isoforms encode truncated versions of a particular septin, which may act as (regulatory) dominant negative forms whose levels might modulate complex formation.
The discrepancy between their observation and our study might stem from different cell lines examined, which might suggest that Akt-mediated phosphorylation of Oct4 at T235 might regulate transcription of stemness genes through modulating Oct4/Sox2 complex formation in a cellular context-dependent manner, and warrants further investigation.
At this level, MAL-bound actin may modulate the formation of ternary complexes of MAL, SRF and DNA, recruit transcriptional repressors or interfere with the formation of active transcription complexes.
However, the role of some residues in SUN-KASH binding was ambiguous in these analyses, perhaps because additional factors that modulate the formation of the LINC complex in vivo were absent or features of the SUN-KASH complex were not accurately represented in the crystal structures.
A promising way to interfere with biological processes is through the control of protein-protein interactions by means of small molecules that modulate the formation of protein-protein complexes.
