Intrinsically disordered proteins and multicellular organisms
- PMID: 25307499
- DOI: 10.1016/j.semcdb.2014.09.025
Intrinsically disordered proteins and multicellular organisms
Abstract
Intrinsically disordered proteins (IDPs) and IDP regions lack stable tertiary structure yet carry out numerous biological functions, especially those associated with signaling, transcription regulation, DNA condensation, cell division, and cellular differentiation. Both post-translational modifications (PTMs) and alternative splicing (AS) expand the functional repertoire of IDPs. Here we propose that an "IDP-based developmental toolkit," which is comprised of IDP regions, PTMs, especially multiple PTMs, within these IDP regions, and AS events within segments of pre-mRNA that code for these same IDP regions, allows functional diversification and environmental responsiveness for molecules that direct the development of complex metazoans.
Keywords: Alternative splicing; Cell cycle; Differentiation; Intrinsic disorder; Post-translational modification; Signaling.
Copyright © 2014 Elsevier Ltd. All rights reserved.
Similar articles
-
The evolutionary origins of cell type diversification and the role of intrinsically disordered proteins.J Exp Bot. 2018 Mar 24;69(7):1437-1446. doi: 10.1093/jxb/erx493. J Exp Bot. 2018. PMID: 29394379 Review.
-
Intrinsically Disordered Proteins Link Alternative Splicing and Post-translational Modifications to Complex Cell Signaling and Regulation.J Mol Biol. 2018 Aug 3;430(16):2342-2359. doi: 10.1016/j.jmb.2018.03.028. Epub 2018 Apr 4. J Mol Biol. 2018. PMID: 29626537
-
Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.J Biol Chem. 2016 Mar 25;291(13):6696-705. doi: 10.1074/jbc.R115.695056. Epub 2016 Feb 5. J Biol Chem. 2016. PMID: 26851279 Free PMC article. Review.
-
Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case.PLoS One. 2016 Jan 7;11(1):e0144284. doi: 10.1371/journal.pone.0144284. eCollection 2016. PLoS One. 2016. PMID: 26742101 Free PMC article.
-
Why do eukaryotic proteins contain more intrinsically disordered regions?PLoS Comput Biol. 2019 Jul 22;15(7):e1007186. doi: 10.1371/journal.pcbi.1007186. eCollection 2019 Jul. PLoS Comput Biol. 2019. PMID: 31329574 Free PMC article.
Cited by
-
Intrinsically Disordered Proteins: Critical Components of the Wetware.Chem Rev. 2022 Mar 23;122(6):6614-6633. doi: 10.1021/acs.chemrev.1c00848. Epub 2022 Feb 16. Chem Rev. 2022. PMID: 35170314 Free PMC article. Review.
-
Muscle developmental defects in heterogeneous nuclear Ribonucleoprotein A1 knockout mice.Open Biol. 2017 Jan;7(1):160303. doi: 10.1098/rsob.160303. Open Biol. 2017. PMID: 28077597 Free PMC article.
-
Anatomy of protein disorder, flexibility and disease-related mutations.Front Mol Biosci. 2015 Aug 12;2:47. doi: 10.3389/fmolb.2015.00047. eCollection 2015. Front Mol Biosci. 2015. PMID: 26322316 Free PMC article.
-
Order, Disorder, and Everything in Between.Molecules. 2016 Aug 19;21(8):1090. doi: 10.3390/molecules21081090. Molecules. 2016. PMID: 27548131 Free PMC article. Review.
-
Evolutionary Study of Disorder in Protein Sequences.Biomolecules. 2020 Oct 6;10(10):1413. doi: 10.3390/biom10101413. Biomolecules. 2020. PMID: 33036302 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials
Miscellaneous