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Intrinsically disordered proteins in cellular signalling and regulation

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 16, Issue 1, Pages 18-29

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3920

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Funding

  1. US National Institutes of Health [CA096865, GM71862]
  2. Skaggs Institute for Chemical Biology
  3. NATIONAL CANCER INSTITUTE [R01CA096865] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM071862] Funding Source: NIH RePORTER

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Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same polypeptide to undertake different interactions with different consequences. IDPs are subject to combinatorial post-translational modifications and alternative splicing, adding complexity to regulatory networks and providing a mechanism for tissue-specific signalling. These proteins participate in the assembly of signalling complexes and in the dynamic self-assembly of membrane-less nuclear and cytoplasmic organelles. Experimental, computational and bioinformatic analyses combine to identify and characterize disordered regions of proteins, leading to a greater appreciation of their widespread roles in biological processes.

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