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Stochastic machines as a colocalization mechanism for scaffold protein function
Author(s) -
Xue Bin,
Romero Pedro R.,
Noutsou Maria,
Maurice Madelon M.,
Rüdiger Stefan G.D.,
William Albert M.,
Mizianty Marcin J.,
Kurgan Lukasz,
Uversky Vladimir N.,
Dunker A. Keith
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.04.006
Subject(s) - colocalization , scaffold protein , mechanism (biology) , function (biology) , biophysics , scaffold , chemistry , phosphorylation , microbiology and biotechnology , casein kinase 2 , gsk 3 , modular design , covalent bond , protein kinase a , biochemistry , computational biology , biology , computer science , physics , signal transduction , mitogen activated protein kinase kinase , organic chemistry , quantum mechanics , database , operating system
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.