Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

Alaji Bah, Robert M. Vernon, Zeba Siddiqui, Mickaël Krzeminski, Ranjith Muhandiram, Charlie Zhao, Nahum Sonenberg, Lewis E. Kay and Julie D. Forman-Kay ()
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Alaji Bah: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Robert M. Vernon: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Zeba Siddiqui: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Mickaël Krzeminski: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Ranjith Muhandiram: University of Toronto, Toronto, Ontario M5S 1A8, Canada
Charlie Zhao: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Nahum Sonenberg: McGill University, Montréal, Quebec H3G 1Y6, Canada
Lewis E. Kay: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada
Julie D. Forman-Kay: Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada

Nature, 2015, vol. 519, issue 7541, 106-109

Abstract: The structural polymorphism of intrinsically disordered protein 4E-BP2 allows it to regulate translation initiation through post-translational modification-mediated folding, exemplifying a new and potentially general mechanism of biological regulation mediated by intrinsically disordered proteins.

Date: 2015
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DOI: 10.1038/nature13999

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