CRIB effector disorder: exquisite function from chaos.
Mott, Helen R
Biochem Soc Trans
Portland Press Ltd.
MetadataShow full item record
Owen, D., & Mott, H. R. (2018). CRIB effector disorder: exquisite function from chaos.. Biochem Soc Trans, 46 (5), 1289-1302. https://doi.org/10.1042/BST20170570
The CRIB (Cdc42/Rac interactive binding) family of small G-protein effectors contain significant regions with intrinsic disorder. The G-protein-binding regions are contained within these intrinsically disordered regions. Most CRIB proteins also contain stretches of basic residues associated with their G-protein-binding regions. The basic region (BR) and G-protein-binding region together allow the CRIB effectors to bind to their cognate G-protein via a dock- and coalesce-binding mechanism. The BRs of these proteins take on multiple roles: steering G-protein binding, interacting with elements of the membrane and regulating intramolecular regulatory interactions. The ability of these regions of the CRIBs to undergo multivalent interactions and mediate charge neutralizations equips them with all the properties required to drive liquid-liquid phase separation and therefore to initiate and drive signalosome formation. It is only recently that the structural plasticity in these proteins is being appreciated as the driving force for these vital cellular processes.
CRIB effectors, intrinsically disordered proteins, protein conformation, small G-proteins, Animals, GTP Phosphohydrolases, GTP-Binding Proteins, Gene Expression Regulation, Humans, Hydrophobic and Hydrophilic Interactions, Membrane Proteins, Nonlinear Dynamics, Polylysine, Protein Binding, Protein Domains, Protein Structure, Quaternary, Signal Transduction, Static Electricity, Tumor Suppressor Proteins, cdc42 GTP-Binding Protein, rac1 GTP-Binding Protein
MRC CASE studentship MR/K017101/1
External DOI: https://doi.org/10.1042/BST20170570
This record's URL: https://www.repository.cam.ac.uk/handle/1810/284747
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