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Title

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

AuthorsDíaz-Moreno, Irene ; Hollingworth, David; Frenkiel, Thomas A.; Kelly, Geoff; Martin, Stephen; Howell, Steven; García-Mayoral, M.F. ; Gherzi, Roberto; Briata, Paola; Ramos, Andrés
KeywordsPhosphorylation
KH
KSRP
AU-rich element
RNA
Molecular
Issue Date8-Feb-2009
PublisherNature Publishing Group
CitationNature Structural and Molecular Biology 16(3): 238-246 (2009)
AbstractThe AU-rich element (ARE)-mediated mRNA-degradation activity of the RNA binding K-homology splicing regulator protein(KSRP) is regulated by phosphorylation of a serine within its N-terminal KH domain (KH1). In the cell, phosphorylation promotes the interaction of KSRP and 14-3-3f protein and impairs the ability of KSRP to promote the degradation of its RNA targets. Here we examine the molecular details of this mechanism. We report that phosphorylation leads to the unfolding of the structurally atypical and unstable KH1, creating a site for 14-3-3f binding. Using this site, 14-3-3f discriminates between phosphorylated and unphosphorylated KH1, driving the nuclear localization of KSRP. 14-3-3f –KH1 interaction regulates the mRNA-decay activity of KSRP by sequestering the protein in a separate functional pool. This study demonstrates how an mRNA-degradation pathway is connected to extracellular signaling networks through the reversible unfolding of a protein domain.
Description9 páginas, 7 figuras, 1 tabla
Publisher version (URL)http://dx.doi.org/10.1038/nsmb.1558
URIhttp://hdl.handle.net/10261/33707
DOI10.1038/nsmb.1558
ISSN1545-9993
Appears in Collections:(IBVF) Artículos
(IQFR) Artículos
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