Phasing in on the cell cycle
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Boeynaems et al. Cell Div (2018) 13:1 https://doi.org/10.1186/s13008-018-0034-4
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COMMENTARY
Phasing in on the cell cycle Steven Boeynaems1,2,3* , Peter Tompa4,5 and Ludo Van Den Bosch1,2
Abstract Just like all matter, proteins can also switch between gas, liquid and solid phases. Protein phase transition has claimed the spotlight in recent years as a novel way of how cells compartmentalize and regulate biochemical reactions. Moreover, this discovery has provided a new framework for the study of membrane-less organelle biogenesis and protein aggregation in neurodegenerative disorders. We now argue that this framework could be useful in the study of cell cycle regulation and cancer. Based on our work on phase transitions of arginine-rich proteins in neurodegeneration, via combining mass spectroscopy with bioinformatics analyses, we found that also numerous proteins involved in the regulation of the cell cycle can undergo protein phase separation. Indeed, several proteins whose function affects the cell cycle or are associated with cancer, have been recently found to phase separate from the test tube to cells. Investigating the role of this process for cell cycle proteins and understanding its molecular underpinnings will provide pivotal insights into the biology of cell cycle progression and cancer. Keywords: Protein phase separation, Oncogenic fusion, Protein aggregation, Cancer, Stress granules, Nucleolus, Centrosome Background Compartmentalization is a key feature of life. The cell membrane defines the context of what is living and what is not. Yet, this is only the first stage of the spatial organization of living matter. Cells, and in particularly eukaryotes, are further divided in subcompartments termed organelles, each of them carrying out specific biochemical reactions. These organelles can be roughly divided in two classes: membrane-bound and membrane-less. Whereas the processes behind the formation of membrane-bound vesicles have been relatively well-studied, the biogenesis and properties of their membrane-less counterparts remained elusive. Membrane-less organelles (e.g. the nucleolus, stress granules, …) often consist of protein and RNA. Yet how does a cell concentrate these biomolecules without a membrane barrier? In recent years the phenomenon of liquid–liquid phase separation was found to underlie the biogenesis of these compartments [1–9]. Multivalent interactions predominantly mediated by intrinsically *Correspondence: steven.boeynaems@vib‑kuleuven.be 1 Department of Neurosciences, Experimental Neurology and Leuven Research Institute for Neuroscience and Disease (LIND), KU LeuvenUniversity of Leuven, 3000 Leuven, Belgium Full list of author information is available at the end of the article
disordered and low complexity domains drive the spontaneous demixing of the RNA binding proteins involved [1–10]. This demixing results in the formation of liquidlike protein droplets or protein hydrogels, and depends on specific in vitro conditions, such as concentration, salt and temperature
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