NDLI: Src tyrosine kinase phosphorylation of nuclear receptor HNF4α correlates with isoform-specific loss of HNF4α in human colon cancer

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Src tyrosine kinase phosphorylation of nuclear receptor HNF4α correlates with isoform-specific loss of HNF4α in human colon cancer

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Src tyrosine kinase phosphorylation of nuclear receptor HNF4α correlates with isoform-specific loss of HNF4α in human colon cancer

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pan, Songqin Chellappa, Karthikeyani Brelivet, Yann Chan, Charles Clarke, Stephen J. Schnabl, Jake M. Sladek, Frances M. Dent, Owen F. Robertson, Graham R. Jankova, Lucy Fung, Caroline L-s
Description	Author Affiliation: Chellappa K ( Department of Cell Biology and Neuroscience, University of California, Riverside, CA 92521, USA.);
Abstract	Src tyrosine kinase has long been implicated in colon cancer but much remains to be learned about its substrates. The nuclear receptor hepatocyte nuclear factor 4α (HNF4α) has just recently been implicated in colon cancer but its role is poorly defined. Here we show that c-Src phosphorylates human HNF4α on three tyrosines in an interdependent and isoform-specific fashion. The initial phosphorylation site is a Tyr residue (Y14) present in the N-terminal A/B domain of P1- but not P2-driven HNF4α. Phospho-Y14 interacts with the Src SH2 domain, leading to the phosphorylation of two additional tyrosines in the ligand binding domain (LBD) in P1-HNF4α. Phosphomimetic mutants in the LBD decrease P1-HNF4α protein stability, nuclear localization and transactivation function. Immunohistochemical analysis of approximately 450 human colon cancer specimens (Stage III) reveals that P1-HNF4α is either lost or localized in the cytoplasm in approximately 80% of tumors, and that staining for active Src correlates with those events in a subset of samples. Finally, three SNPs in the human HNF4α protein, two of which are in the HNF4α F domain that interacts with the Src SH3 domain, increase phosphorylation by Src and decrease HNF4α protein stability and function, suggesting that individuals with those variants may be more susceptible to Src-mediated effects. This newly identified interaction between Src kinase and HNF4α has important implications for colon and other cancers.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	109
Language	English
Publisher	National Academy of Sciences
Publisher Date	2012-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Nucleus Metabolism Colonic Neoplasms Enzymology Hepatocyte Nuclear Factor 4 Protein Isoforms Src-Family Kinases Cell Line Pathology Genetics Molecular Mimicry Phosphorylation Polymorphism, Single Nucleotide Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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