Abstract
The nucleoli of Dictyostelium discoideum have a comparatively unique, non-canonical, localization adjacent to the inner nuclear membrane. The verified nucleolar proteins of this eukaryotic microbe are detailed while other potential proteins are introduced. Heat shock protein 32 (Hsp32), eukaryotic translation initiation factor 6 (eIF6), and tumour necrosis factor receptor-associated protein 1 (TRAP1) are essential for cell survival. NumA1, a breast cancer type 1 susceptibility protein-C Terminus domain-containing protein linked to cell cycle, functions in the regulation of nuclear number. The cell cycle checkpoint kinase 2 homologue forkhead-associated kinase A (FhkA) and BRG1-associated factor 60a homologue Snf12 are also discussed. While nucleoli appear homogeneous ultrastructurally, evidence for nucleolar subcompartments exists. Nucleolar localization sequences (NoLS) have been defined that target proteins to either the general nucleolar area or to a specific intranucleolar domain. Protein translocations during mitosis are protein-specific and support the multiple functions of the Dictyostelium nucleolus. To enrich the picture, binding partners of NumA1, the most well-characterized nucleolar protein, are examined: nucleolar Ca2+-binding protein 4a (CBP4a), nuclear puromycin-sensitive aminopeptidase A (PsaA) and Snf12. The role of Dictyostelium as a model for understanding the contribution of nucleolar proteins to various diseases and cellular stress is discussed throughout the review.
Highlights
The nucleolus is a multifunctional subnuclear compartment that has been studied for more than 200 years [1,2]
Studies have primarily focused on the transcription of rDNA genes and rRNA processing leading to the assembly of ribosomal subunits that are exported to the cytoplasm
In total the results indicate that Calcium Binding Protein 4a (Cbp4a) localizes
Summary
The nucleolus is a multifunctional subnuclear compartment that has been studied for more than 200 years [1,2]. Studies have primarily focused on the transcription of rDNA genes and rRNA processing leading to the assembly of ribosomal subunits that are exported to the cytoplasm These functions underlie the basic structure and organization of eukaryotic bipartite or tripartite nucleoli. Despite the early interest in ribosome biogenesis, about 70% of the nucleolar proteome functions in other events including cell signaling, centrosome function, chaperone activity, DNA replication and repair, molecular sequestration, regulation of cell cycle events, stress response regulation and viral replication [3,4] This diversity of functions underlies the central role of the nucleolus in a diversity of human diseases [1,2]. In the last decade or so, Dictyostelium has gained prominence for the study of cell of cell stress as well as human diseases including Batten’s disease, host-pathogen interactions, and stress as well as human diseases including Batten’s disease, host-pathogen interactions, and Huntington’s disease [6]
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