SHP2 Tyrosine Phosphatase Converts Parafibromin/Cdc73 from a Tumor Suppressor to an Oncogenic Driver

• Published in: Molecular cell Vol. 43; no. 1; pp. 45 - 56
• Main Authors: Takahashi, Atsushi, Tsutsumi, Ryouhei, Kikuchi, Ippei, Obuse, Chikashi, Saito, Yasuhiro, Seidi, Azadeh, Karisch, Robert, Fernandez, Minerva, Cho, Taewoo, Ohnishi, Naomi, Rozenblatt-Rosen, Orit, Meyerson, Matthew, Neel, Benjamin G., Hatakeyama, Masanori
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08.07.2011
• Subjects: abnormal development; Animals; beta Catenin - metabolism; Cell Nucleus - metabolism; cell physiology; Cercopithecus aethiops; COS Cells; Cyclin D1 - genetics; Cyclin D1 - metabolism; cyclins; dephosphorylation; DNA-directed RNA polymerase; Gene Expression Regulation; genes; HEK293 Cells; histones; Humans; malformations; Mass Spectrometry; methyltransferases; Mice; Mice, Inbred C57BL; neoplasms; Phosphorylation; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - analysis; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - physiology; Proto-Oncogene Proteins c-myc - genetics; Proto-Oncogene Proteins c-myc - metabolism; RNA; Signal Transduction; signals; Tumor Suppressor Proteins - genetics; Tumor Suppressor Proteins - metabolism; Tumor Suppressor Proteins - physiology; tyrosine; Tyrosine - metabolism; Wnt Proteins - metabolism

Deregulation of SHP2 is associated with malignant diseases as well as developmental disorders. Although SHP2 is required for full activation of RAS signaling, other potential roles in cell physiology have not been elucidated. Here we show that SHP2 dephosphorylates parafibromin/Cdc73, a core compone...