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.

The mitotic exit network signals from spindle pole bodies to the nucleolus through the dynamic localization of its terminal kinase complex Dbf2-Mob1.

Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.

Forcing protein associations across the proteome reveals the cell's tolerance for diverse protein interactions and reveals the interactions that affect growth.

Single molecule FISH analysis defines the behavior of centromere-derived alpha-satellite transcripts in intact human cells and reveals a critical role for centromere-nucleolar contacts in repressing alpha-satellite transcription.

The mitotic chromosome periphery is organised by the PP1 binding protein Ki-67 and contributes to nucleolar re-activation upon mitotic exit.

The chaperones Hsp70 and Sis1 collaborate to repress the heat shock response and are both transcriptional targets of the heat shock response, yet only Hsp70 acts as a negative feedback regulator of the heat shock response.

The interaction between rDNA instability and proteostasis stress, two major aging hallmarks, underlies single-cell aging trajectories in yeast.

Antigen Ki-67, which is widely used as a cell proliferation marker, controls heterochromatin organisation and gene expression.

A novel family of nucleolus-enriched ncRNAs forms allele-specific territories on the nucleolar organizing region (NOR)-containing acrocentric chromosomes.