Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 44, Issue -, Pages 1185-1200Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST20160172
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Funding
- Medical Research Council [MC_U105185859]
- EMBO
- HFSP
- BBSRC/ERASysBio+
- Royal Society
- Trinity College
- Darwin College
- Lister Institute Research Prize
- Medical Research Council [MC_U105185859] Funding Source: researchfish
- MRC [MC_U105185859] Funding Source: UKRI
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In the 1960s, Christian Anfinsen postulated that the unique three-dimensional structure of a protein is determined by its amino acid sequence. This work laid the foundation for the sequence-structure-function paradigm, which states that the sequence of a protein determines its structure, and structure determines function. However, a class of polypeptide segments called intrinsically disordered regions does not conform to this postulate. In this review, I will first describe established and emerging ideas about how disordered regions contribute to protein function. I will then discuss molecular principles by which regulatory mechanisms, such as alternative splicing and asymmetric localization of transcripts that encode disordered regions, can increase the functional versatility of proteins. Finally, I will discuss how disordered regions contribute to human disease and the emergence of cellular complexity during organismal evolution.
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