Heterogeneous nuclear ribonucleoprotein Q is a novel substrate of SH2 domain-containing phosphatase-2.
SH2 domain-containing phosphatase-2 (SHP2) is a protein-tyrosine phosphatase implicated in activation of cell signalling such as the Ras/extracellular signal-regulated kinase pathway. The substrates of SHP2 and their roles in cell activation are not fully understood. By using the substrate-trapping method with the phosphatase-dead SHP2 mutant, in which C459 was substituted by serine, and the matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometric analysis, we found that heterogeneous nuclear ribonucleoprotein Q (hnRNP Q), a protein implicated in RNA metabolisms, was a novel substrate of SHP2. Tyrosine-phosphorylated hnRNP Q was detected in HL-60, Jurkat and human peripheral blood mononuclear cells, but not mature neutrophils, treated with pervanadate. Tyrosine-phosphorylated hnRNP Q was directly bound to SHP2 in vivo and in vitro, and dephosphorylated by SHP2 in vitro. These findings suggest that hnRNP Q is a novel substrate of SHP2 and the SHP2 activity may be also involved in RNA metabolisms via dephosphorylation of hnRNP Q.
['Watanabe|Norifumi|N|', 'Kato|Takayuki|T|', 'Fujita|Hisakazu|H|', 'Kitagawa|Seiichi|S|']
D057809:HEK293 Cells D018922:HL-60 Cells D034441:Heterogeneous-Nuclear Ribonucleoproteins D006801:Humans D019169:Jurkat Cells D007963:Leukocytes, Mononuclear D013058:Mass Spectrometry D010766:Phosphorylation D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11 D012313:RNA
heterogeneous nuclear ribonucleoprotein Q SH2 domain-containing phosphatase-2 pervanadate