CPEB4's switch from translational repressor to activator is regulated during cell cycle by hyperphosphorylation of its intrinsically disordered domain, which controls its phase-separation into RNA-containing liquid-like droplets.
Binding of multiple LC8 copies to the intrinsically disordered region of the transcription factor ASCIZ exemplifies a new and potentially widespread molecular mechanism for negative feedback regulation.
Nucleolar protein localization involves the phase separation within the nucleolar matrix via three types of multivalent features: acidic tracts, nucleic acid binding domains and arginine-rich low complexity sequences.
GCNA proteins comprise a previously unnoticed family of proteins that has been enriched in cells carrying a heritable genome since the invention of sexual reproduction in eukaryotes, and has had reproductive function for at least 600 million years.
Structural and biochemical analysis reveals that two intrinsically disordered domains of the transcription factor FoxM1 co-fold to form an autoinhibited conformation, which is disrupted by a specific activating phosphorylation event.
Modeling and biophysics show that the unstructured acidic tail of the Sm protein Hfq mimics nucleic acid to auto inhibit its chaperone activity, preventing Hfq from being sequestered by inauthentic substrates and providing insight into the evolution of Hfq's chaperone function among bacterial genera.
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