Physical and functional interactions between HNF4A and TAF4 coordinate HNF4A genomic occupancy with pre-initiation complex formation to activate post-natal hepatocyte gene expression.
The small molecule, 147, is a pro-drug that preferentially activates ATF6 signaling through a mechanism involving localized metabolic activation and selective covalent modification of ER resident proteins involved in regulating ATF6 activity.
Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex
The Wtf4 antidote protein assembles with the Wtf4 poison protein and promotes the transportation of the assembled proteins to the vacuole for sequestration or destruction.
The transcription factor C/EBPβ binds to different DNA sequences depending on whether it binds to ATF4, which enables C/EBPβ to conduct diverse transcriptional programs during adipocyte differentiation by exploiting an expanded motif repertoire.
The heme and HRI-mediated eIF2aP–ATF4 integrated stress response in erythropoiesis has a major global impact, especially under the stress condition of iron deficiency.
Integrated stress response-induced expression of ATF4 and its transactivation of SOX9 causes aberrant chondrocyte differentiation and skeletal defects which can be alleviated by modulating initiation-factor eIF2α phosphorylation translation control.
