RET oncoproteins induce tyrosine phosphorylation changes of proteins involved in RNA metabolism.
Cell Signal
; 18(12): 2272-82, 2006 Dec.
Article
em En
| MEDLINE
| ID: mdl-16843637
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.
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Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
RNA
/
Proteínas
/
Proteínas Proto-Oncogênicas c-ret
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article