PR55α-containing protein phosphatase 2A complexes promote cancer cell migration and invasion through regulation of AP-1 transcriptional activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-03

AUTHORS

O Gilan, J Diesch, M Amalia, K Jastrzebski, A C Chueh, N M Verrills, R B Pearson, J M Mariadason, E Tulchinsky, R D Hannan, A S Dhillon

ABSTRACT

The proto-oncogene c-Jun is a component of activator protein-1 (AP-1) transcription factor complexes that regulates processes essential for embryonic development, tissue homeostasis and malignant transformation. Induction of gene expression by c-Jun involves stimulation of its transactivation ability and upregulation of DNA binding capacity. While it is well established that the former requires JNK-mediated phosphorylation of S63/S73, the mechanism(s) through which binding of c-Jun to its endogenous target genes is regulated remains poorly characterized. Here we show that interaction of c-Jun with chromatin is positively regulated by protein phosphatase 2A (PP2A) complexes targeted to c-Jun by the PR55α regulatory subunit. PR55α-PP2A specifically dephosphorylates T239 of c-Jun, promoting its binding to genes regulating tumour cell migration and invasion. PR55α-PP2A also enhanced transcription of these genes, without affecting phosphorylation of c-Jun on S63. These findings suggest a critical role for interplay between JNK and PP2A pathways determining the functional activity of c-Jun/AP-1 in tumour cells. More... »

PAGES

1333

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/onc.2014.26

DOI

http://dx.doi.org/10.1038/onc.2014.26

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006422062

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24632621


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