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Cell Signal. 2006 Dec;18(12):2272-82. Epub 2006 May 24.

RET oncoproteins induce tyrosine phosphorylation changes of proteins involved in RNA metabolism.

Author information

1
Proteomics Laboratory, Department of Experimental Oncology and Lab. Istituto Nazionale Tumori, Via G. Venezian 1, 20133 Milan Italy.

Abstract

We report the identification of proteins induced in response to RET/PTC2, an oncogene implicated in thyroid cancers. Anti-phosphotyrosine antibody affinity resin was used to purify Tyr(P)-containing and interacting proteins from 293T and NIH3T3 cells which were transfected with kinase active or inactive RET/PTC and RETMEN2 oncogenes. Proteins were separated by one-dimensional SDS-PAGE, extracted by in-gel digestion, and identified by MALDI-TOF peptide mass fingerprinting. The expression and tyrosine phosphorylation of Sam68, a protein implicated in mRNA nucleocytoplasmic translocation and splicing, were further examined in RET-transfected cells and thyroid tumors. Of relevance, cells transfected with RETMEN2B examined for anti-phosphotyrosine bound proteins, showed other proteins implicated in splicing: DEAD-box p68 RNA helicase, SYNCRIP, and hnRNP K. Western blotting analysis suggested that these proteins are singularly tyrosine phosphorylated in RETMEN2B-transfected cells, and that they constitutively bind with Sam68. The study concludes that regulation of splicing factors is likely to be important in RET-mediated thyroid carcinogenesis.

PMID:
16843637
DOI:
10.1016/j.cellsig.2006.05.016
[Indexed for MEDLINE]

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