Nucleocytoplasmic protein translocation during mitosis in the social amoebozoan <i>Dictyostelium discoideum</i>

O’Day, Danton H.; Budniak, Aldona

doi:10.1111/brv.12100

Cited by 8 publications

(9 citation statements)

References 132 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of CaM in the nucleus of this microbe has been experimentally verified (Huber, Catalano, & O'Day, ). The cell cycle includes semi‐closed mitosis wherein the nuclear envelope does not break down but allows the regulated nucleocytoplasmic transport of various CaMBPs and some of their binding partners (O'Day & Budniak, ). For example, cyclin‐dependent kinase 5 (Cdk5) is a nuclear CaMBP that progressively translocates from the nucleoplasm to the cytoplasm during mitosis, re‐entering the nucleus during cytokinesis (Huber et al, ).…”

Section: Growth Phase and Semi‐closed Mitosismentioning

confidence: 99%

“…Unlike NumA, PsaA and Cdk5 that translocate from the nucleus to the cytoplasm during mitosis, Cbp4a localizes to the nucleoplasm after nucleolar dissolution where it organizes into multiple, discrete nucleoplasmic islands (Catalano & O'Day, ; O'Day, ). These translocations along with those of other proteins led to the realization that D. discoideum has a semi‐open mitosis as opposed to a closed mitosis as previously thought (O'Day & Budniak, ). Semi‐open mitosis refers to a form of mitosis in which the nuclear envelope undergoes fenestration to be partially but not completely disrupted.…”

Section: Growth Phase and Semi‐closed Mitosismentioning

confidence: 99%

See 1 more Smart Citation

Calmodulin‐mediated events during the life cycle of the amoebozoan Dictyostelium discoideum

et al. 2019

Self Cite

View full text Add to dashboard Cite

This review focusses on the functions of intracellular and extracellular calmodulin, its target proteins and their binding proteins during the asexual life cycle of Dictyostelium discoideum. Calmodulin is a primary regulatory protein of calcium signal transduction that functions throughout all stages. During growth, it mediates autophagy, the cell cycle, folic acid chemotaxis, phagocytosis, and other functions. During mitosis, specific calmodulin‐binding proteins translocate to alternative locations. Translocation of at least one cell adhesion protein is calmodulin dependent. When starved, cells undergo calmodulin‐dependent chemotaxis to cyclic AMP generating a multicellular pseudoplasmodium. Calmodulin‐dependent signalling within the slug sets up a defined pattern and polarity that sets the stage for the final events of morphogenesis and cell differentiation. Transected slugs undergo calmodulin‐dependent transdifferentiation to re‐establish the disrupted pattern and polarity. Calmodulin function is critical for stalk cell differentiation but also functions in spore formation, events that begin in the pseudoplasmodium. The asexual life cycle restarts with the calmodulin‐dependent germination of spores. Specific calmodulin‐binding proteins as well as some of their binding partners have been linked to each of these events. The functions of extracellular calmodulin during growth and development are also discussed. This overview brings to the forefront the central role of calmodulin, working through its numerous binding proteins, as a primary downstream regulator of the critical calcium signalling pathways that have been well established in this model eukaryote. This is the first time the function of calmodulin and its target proteins have been documented through the complete life cycle of any eukaryote.

show abstract

Section: Growth Phase and Semi‐closed Mitosismentioning

confidence: 99%

Section: Growth Phase and Semi‐closed Mitosismentioning

confidence: 99%

Calmodulin‐mediated events during the life cycle of the amoebozoan Dictyostelium discoideum

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

“…discoideum mitosis is a semi-open process [30], we further studied the localization of DdNKAP during mitosis. AX2 cells expressing GFP-DdNKAP were fixed after release from a nocodazole block.…”

Section: Resultsmentioning

confidence: 99%

The C-Terminal SynMuv/DdDUF926 Domain Regulates the Function of the N-Terminal Domain of DdNKAP

et al. 2016

View full text Add to dashboard Cite

NKAP (NF-κB activating protein) is a highly conserved SR (serine/arginine-rich) protein involved in transcriptional control and splicing in mammals. We identified DdNKAP, the Dictyostelium discoideum ortholog of mammalian NKAP, as interacting partner of the nuclear envelope protein SUN-1. DdNKAP harbors a number of basic RDR/RDRS repeats in its N-terminal domain and the SynMuv/DUF926 domain at its C-terminus. We describe a novel and direct interaction between DdNKAP and Prp19 (Pre mRNA processing factor 19) which might be relevant for the observed DdNKAP ubiquitination. Genome wide analysis using cross-linking immunoprecipitation-high-throughput sequencing (CLIP-seq) revealed DdNKAP association with intergenic regions, exons, introns and non-coding RNAs. Ectopic expression of DdNKAP and its domains affects several developmental aspects like stream formation, aggregation, and chemotaxis. We conclude that DdNKAP is a multifunctional protein, which might influence Dictyostelium development through its interaction with RNA and RNA binding proteins. Mutants overexpressing full length DdNKAP and the N-terminal domain alone (DdN-NKAP) showed opposite phenotypes in development and opposite expression profiles of several genes and rRNAs. The observed interaction between DdN-NKAP and the DdDUF926 domain indicates that the DdDUF926 domain acts as negative regulator of the N-terminus.

show abstract

“…Moreover, during mitosis these proteins each exhibit a unique pattern of redistribution [15][16][17]. Dictyostelium undergoes a semi-open mitosis and the nucleocytoplasmic translocation of all known nuclear proteins, including those in the nucleolus, has recently been reviewed [27]. This diversity in localization patterns suggests diversity in function.…”

Section: Discussionmentioning

confidence: 99%

Evidence for nucleolar subcompartments in Dictyostelium

Catalano

O’Day

2015

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

The nucleolus is a multifunctional nuclear compartment usually consisting of two to three subcompartments which represent stages of ribosomal biogenesis. It is linked to several human diseases including viral infections, cancer, and neurodegeneration. Dictyostelium is a model eukaryote for the study of fundamental biological processes as well as several human diseases however comparatively little is known about its nucleolus. Unlike most nucleoli it does not possess visible subcompartments at the ultrastructural level. Several recently identified nucleolar proteins in Dictyostelium leave the nucleolus after treatment with the rDNA transcription inhibitor actinomycin-D (AM-D). Different proteins exit in different ways, suggesting that previously unidentified nucleolar subcompartments may exist. The identification of nucleolar subcompartments would help to better understand the nucleolus in this model eukaryote. Here, we show that Dictyostelium nucleolar proteins nucleomorphin isoform NumA1 and Bud31 localize throughout the entire nucleolus while calcium-binding protein 4a localizes to only a portion, representing nucleolar subcompartment 1 (NoSC1). SWI/SNF complex member Snf12 localizes to a smaller area within NoSC1 representing a second nucleolar subcompartment, NoSC2. The nuclear/nucleolar localization signal KRKR from Snf12 localized GFP to NoSC2, and thus also appears to function as a nucleolar subcompartment localization signal. FhkA localizes to the nucleolar periphery displaying a similar pattern to that of Hsp32. Similarities between the redistribution patterns of Dictyostelium nucleolar proteins during nucleolar disruption as a result of either AM-D treatment or mitosis support these subcompartments. A model for the AM-D-induced redistribution patterns is proposed.

show abstract

Nucleocytoplasmic protein translocation during mitosis in the social amoebozoan Dictyostelium discoideum

Cited by 8 publications

References 132 publications

Calmodulin‐mediated events during the life cycle of the amoebozoan Dictyostelium discoideum

Calmodulin‐mediated events during the life cycle of the amoebozoan Dictyostelium discoideum

The C-Terminal SynMuv/DdDUF926 Domain Regulates the Function of the N-Terminal Domain of DdNKAP

Evidence for nucleolar subcompartments in Dictyostelium

Contact Info

Product

Resources

About