Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding

被引：0

作者：

Irene Díaz-Moreno

David Hollingworth

Thomas A Frenkiel

Geoff Kelly

Stephen Martin

Steven Howell

MaríaFlor García-Mayoral

Roberto Gherzi

Paola Briata

Andres Ramos

机构：

[1] MRC National Institute for Medical Research,Molecular Structure Division

[2] The Ridgeway,Physical Biochemistry Division

[3] Mill Hill,undefined

[4] MRC Biomedical NMR Centre,undefined

[5] The Ridgeway,undefined

[6] Mill Hill,undefined

[7] MRC National Institute for Medical Research,undefined

[8] The Ridgeway,undefined

[9] Mill Hill,undefined

[10] Istituto Nazionale per la Ricerca sul Cancro,undefined

[11] Largo Benzi Rosanna,undefined

[12] 10,undefined

[13] Instituto de Bioquímica Vegetal y Fotosíntesis,undefined

[14] US-CSIC,undefined

[15] Avda. Americo Vespucio 49,undefined

来源：

Nature Structural & Molecular Biology | 2009年 / 16卷

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D O I：

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学科分类号：

摘要：

KSRP is involved in mRNA instability, a role that is repressed upon AKT kinase–mediated phosphorylation, which promotes 14-3-3 interaction. This modification site is now shown to be exposed upon AKT phosphorylation through unfolding of the KH1 domain of KSRP, an event that allows 14-3-3 interaction, which in turn affects nuclear cytoplasmic partitioning.

引用

页码：238 / 246

页数：8

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