Publication Date:
2013-10-29
Description:
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.
Print ISSN:
0021-924X
Electronic ISSN:
1756-2651
Topics:
Biology
,
Chemistry and Pharmacology
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