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- W1657340524 abstract "Cellular “bodies”, i.e. organelles in cells that are not enclosed by membranes, have been characterized as large protein assemblies with liquid-like properties, though the biophysical basis for their formation is currently unclear. Recent work demonstrated that weak, multivalent protein interactions can result in the formation of large higher-order complexes, can undergo liquid demixing phase separation in vitro and may enable the formation of cellular bodies. The inherent size heterogeneity of higher-order complexes renders them difficult to characterize biophysically and structurally. As a result, their size distributions remain largely unquantified, limiting molecular insight into their biological functions. We report novel mechanisms governing the formation of nuclear SPOP bodies and stress granules in which the self-association of folded domains into large homo-oligomers and of long disordered regions play key roles. We have used biophysical, biochemical and cell biological approaches to explore the self-association of proteins in vitro, to quantify the size distribution of the resulting higher-order oligomers, and to relate these to the function of cellular bodies in cells. We further explore how changes in self-association properties of constituent proteins, i.e. the destabilization or rigidification of cellular bodies, can lead to cancer and neurodegenerative diseases. We propose that dynamic, higher-order protein self-association is a general mechanism underlying the formation of cellular bodies. These may serve as hotspots of enzymatic or signaling activity, which can be dynamically turned on or off through the regulated assembly and disassembly of the organelle bodies, respectively." @default.
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- W1657340524 date "2015-01-01" @default.
- W1657340524 modified "2023-09-28" @default.
- W1657340524 title "The Role of Protein Disorder and Self-Association in the Formation of Cellular Bodies" @default.
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- W1657340524 doi "https://doi.org/10.1016/j.bpj.2014.11.047" @default.
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