Journal
FEBS JOURNAL
Volume 276, Issue 19, Pages 5390-5405Publisher
WILEY
DOI: 10.1111/j.1742-4658.2009.07251.x
Keywords
interaction specificity; intrinsically unstructured proteins; linear motifs; modular recognition domains; peptide-mediated interactions; phosphorylation events; post-translational modifications; protein disorder; protein interaction networks; signalling networks
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Funding
- Spanish Ministerio de Educacion y Ciencia [BIO2007-62426, BIO2007-63458]
- European Commission [LSHG-CT-2005-512028]
- FPU fellowship
- Spanish Ministerio de Ciencia y Innovacion
- Generalitat Catalunya
- ICREA Funding Source: Custom
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Virtually every process in a cell is carried out by macromolecular complexes whose actions need to be perfectly orchestrated. The synchronization and regulation of these biological functions is indeed critical and is usually carried out by complex networks of transient protein interactions. Here, we review some of the many strategies that proteins in regulatory networks use to achieve the dynamic plasticity necessary to rapidly respond to diverse cellular needs. More specifically, we present recent work on the molecular bases of transient peptide-mediated interactions and the role that post-translational modifications and disordered regions might play. Finally, in light of some recent findings, we speculate on the possibility of a new regulatory code for intrinsically disordered proteins and the potential biophysical and functional advantages that disorder might provide.
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