The University of Southampton
University of Southampton Institutional Repository

The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha

Buxade, Maria, Morrice, Nick, Proud, Christopher G. and Krebs, Danielle L. (2008) The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha The Journal of Biological Chemistry, 283, (1), pp. 57-65. (doi:10.1074/jbc.M705286200). (PMID:17965020).

Record type: Article

Abstract

To identify new potential substrates for the MAP kinase signal-integrating kinases (Mnks), we employed a proteomic approach. The Mnks are targeted to the translational machinery through their interaction with the cap-binding initiation factor complex. We tested whether proteins retained on cap resin were substrates for the Mnks in vitro, and identified one such protein as PSF (the PTB (polypyrimidine tract-binding protein)-associated splicing factor). Mnks phosphorylate PSF at two sites in vitro, and our data show that PSF is an Mnk substrate in vivo. We also demonstrate that PSF, together with its partner, p54nrb, binds RNAs that contain AU-rich elements (AREs), such as those for proinflammatory cytokines (e.g. tumor necrosis factor ? (TNF?)). Indeed, PSF associates specifically with the TNF? mRNA in living cells. PSF is phosphorylated at two sites by the Mnks. Our data show that Mnk-mediated phosphorylation increases the binding of PSF to the TNF? mRNA in living cells. These findings identify a novel Mnk substrate. They also suggest that the Mnk-catalyzed phosphorylation of PSF may regulate the fate of specific mRNAs by modulating their binding to PSF·p54nrb.

PDF J._Biol._Chem.-2008-Buxadé-57-65.pdf - Version of Record
Download (507kB)

More information

e-pub ahead of print date: 26 October 2007
Published date: 4 January 2008

Identifiers

Local EPrints ID: 159295
URI: http://eprints.soton.ac.uk/id/eprint/159295
ISSN: 0021-9258
PURE UUID: a2f3e3a3-d057-468c-9a13-43d27ccda84b

Catalogue record

Date deposited: 30 Jun 2010 10:03
Last modified: 18 Jul 2017 12:37

Export record

Altmetrics

Contributors

Author: Maria Buxade
Author: Nick Morrice
Author: Christopher G. Proud
Author: Danielle L. Krebs

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×