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Dynamic complexes of intrinsically disordered proteins and their regulation by post‐translational modifications
Author(s) -
FormanKay Julie D
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.459.1
Subject(s) - flexibility (engineering) , posttranslational modification , intrinsically disordered proteins , translation (biology) , organelle , function (biology) , translational regulation , phosphorylation , biophysics , microbiology and biotechnology , chemistry , computational biology , biology , biochemistry , messenger rna , enzyme , statistics , mathematics , gene
Intrinsically disordered proteins play a significant role in mediating protein interactions in biology. These binding events can involve disorder‐to‐order transitions of various degrees but many complexes retain significant flexibility within “fuzzy” or dynamic complexes. Examples of dynamic interactions regulated by phosphorylation or other post‐translational modifications of the disordered protein will be presented and the evidence for flexibility in the complexes highlighted. Included will be interactions that regulate cell cycle, ion flux, translation and embryogenesis, the latter involving large scale self‐association of the disordered protein into liquid‐like phase separated organelles. Importantly, the function of the binding/association, the post‐translational modification and the dynamics varies in each of these different systems. Links between the flexibility and function of the complex in these examples will be discussed.