Stochastic Machines as a Colocalization Mechanism for Scaffold Protein Function
Document Type
Article
Publication Date
2013
Keywords
Scaffold Proteins, Molecular Machines, Signaling, Protein Complexes
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.febslet.2013.04.006
Abstract
The axis inhibition (Axin) scaffold protein colocalizes β-catenin, casein kinase Iα, and glycogen synthetase kinase 3β by their binding to Axin’s long intrinsically disordered region, thereby yielding structured domains with flexible linkers. This complex leads to the phosphorylation of β-catenin, marking it for destruction. Fusing proteins with flexible linkers vastly accelerates chemical interactions between them by their colocalization. Here we propose that the complex works by random movements of a “stochastic machine,” not by coordinated conformational changes. This non-covalent, modular assembly process allows the various molecular machine components to be used in multiple processes.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 587, issue 11, p. 1587-1591
Scholar Commons Citation
Xue, Bin; Romero, Pedro R.; Noutsou, Maria; Maurice, Madelon M.; Rüdiger, Stefan G.D.; William, Albert M. Jr.; Mizianty, Marcin J.; Kurgan, Lukasz; Uversky, Vladimir N.; and Dunker, A. Keith, "Stochastic Machines as a Colocalization Mechanism for Scaffold Protein Function" (2013). Molecular Medicine Faculty Publications. 529.
https://digitalcommons.usf.edu/mme_facpub/529
