<HashMap><database>biostudies-other</database><scores/><additional><omics_type>Unknown</omics_type><volume>110</volume><submitter>Lucian Smith</submitter><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>E2934-43</pagination><species>Homo sapiens</species><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/MODEL1410300001</full_dataset_link><repository>biostudies-other</repository><additional_accession>23847209</additional_accession><pubmed_authors>Dirk Fey</pubmed_authors><pubmed_authors>Lucian Smith</pubmed_authors></additional><is_claimable>false</is_claimable><name>Reiterer2013 - pseudophosphatase STYX role in ERK signalling</name><description>&lt;notes xmlns="http://www.sbml.org/sbml/level2/version4">      &lt;body xmlns="http://www.w3.org/1999/xhtml">        &lt;div class="dc:title">Reiterer2013 - pseudophosphatase STYX role inERK signalling&lt;/div>&lt;div class="dc:bibliographicCitation">  &lt;p>This model is described in the article:&lt;/p>  &lt;div class="bibo:title">    &lt;a href="http://identifiers.org/pubmed/23847209" title="Access to this publication">Pseudophosphatase STYX    modulates cell-fate decisions and cell migration by    spatiotemporal regulation of ERK1/2.&lt;/a>  &lt;/div>  &lt;div class="bibo:authorList">Reiterer V, Fey D, Kolch W,  Kholodenko BN, Farhan H.&lt;/div>  &lt;div class="bibo:Journal">Proc. Natl. Acad. Sci. U.S.A. 2013 Jul;  110(31): E2934-43&lt;/div>  &lt;p>Abstract:&lt;/p>  &lt;div class="bibo:abstract">    &lt;p>Serine/threonine/tyrosine-interacting protein (STYX) is a    catalytically inactive member of the dual-specificity    phosphatases (DUSPs) family. Whereas the role of DUSPs in    cellular signaling is well explored, the function of STYX is    still unknown. Here, we identify STYX as a spatial regulator of    ERK signaling. We used predictive-model simulation to test    several hypotheses for possible modes of STYX action. We show    that STYX localizes to the nucleus, competes with nuclear DUSP4    for binding to ERK, and acts as a nuclear anchor that regulates    ERK nuclear export. Depletion of STYX increases ERK activity in    both cytosol and nucleus. Importantly, depletion of STYX causes    an ERK-dependent fragmentation of the Golgi apparatus and    inhibits Golgi polarization and directional cell migration.    Finally, we show that overexpression of STYX reduces ERK1/2    activation, thereby blocking PC12 cell differentiation.    Overall, our results identify STYX as an important regulator of    ERK1/2 signaling critical for cell migration and PC12 cell    differentiation.&lt;/p>  &lt;/div>&lt;/div>&lt;div class="dc:publisher">  &lt;p>This model is hosted on   &lt;a href="http://www.ebi.ac.uk/biomodels/">BioModels Database&lt;/a>  and identified by:   &lt;a href="http://identifiers.org/biomodels.db/BIOMD0000000557">BIOMD0000000557&lt;/a>.&lt;/p>  &lt;p>To cite BioModels Database, please use:   &lt;a href="http://identifiers.org/pubmed/20587024" title="Latest BioModels Database publication">BioModels Database:  An enhanced, curated and annotated resource for published  quantitative kinetic models&lt;/a>.&lt;/p>&lt;/div>&lt;div class="dc:license">  &lt;p>To the extent possible under law, all copyright and related or  neighbouring rights to this encoded model have been dedicated to  the public domain worldwide. Please refer to   &lt;a href="http://creativecommons.org/publicdomain/zero/1.0/" title="Access to: CC0 1.0 Universal (CC0 1.0), Public Domain Dedication">CC0  Public Domain Dedication&lt;/a> for more information.&lt;/p>&lt;/div>&lt;/body>    &lt;/notes></description><dates><release>2014-10-30T00:00:00Z</release><modification>2025-07-15T10:01:06.215Z</modification><creation>2025-03-29T17:53:35.59Z</creation></dates><accession>MODEL1410300001</accession><cross_references><biomodels___db>BIOMD0000000557</biomodels___db><pubmed>23847209</pubmed><mamo>MAMO_0000046</mamo><go>GO:0070372</go><go>GO:0005634</go><go>GO:0005829</go><taxonomy>9606</taxonomy><bto>BTO:0000567</bto><uniprot>Q13115</uniprot><uniprot>P27361</uniprot><uniprot>Q02750</uniprot><uniprot>Q8WUJ0</uniprot></cross_references></HashMap>