TAILIEUCHUNG - Báo cáo khoa học: Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit, a4 and the mammalian ortholog of yeast Tip41 (TIPRL)

Type 2A serine⁄threonine phosphatases are part of the PPP subfamily that is formed by PP2A, PP4 and PP6, and participate in a variety of cellular processes including transcription, translation, regulation of the cell cycle, signal transduction and apoptosis. | ỊFEBS Journal Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit a4 and the mammalian ortholog of yeast Tip41 TIPRL Juliana H. C. Smetana and Nilson I. T. Zanchin Center for StructuralMolecular Biology Brazilian Synchrotron Light Laboratory LNLS Campinas Brazil Keywords a4 rapamycin pathway Tip41 type 2A phosphatases yeast two-hybrid system Correspondence N. I. T. Zanchin Centro de Biologia Molecular Estrutural Laboratorio Nacional de Luz Síncrotron R. Giuseppe Maximo Scolfaro Campinas - SP PO Box 6192 CEP 13084-971 Brazil Fax 55 19 3512 1004 Tel 55 19 3512 1113 E-mail zanchin@ Received 7 June 2007 revised 25 August 2007 accepted 20 September 2007 doi Type 2A serine threonine phosphatases are part of the PPP subfamily that is formed by PP2A PP4 and PP6 and participate in a variety of cellular processes including transcription translation regulation of the cell cycle signal transduction and apoptosis. PP2A is found predominantly as a heterotrimer formed by the catalytic subunit C and by a regulatory B B or B and a scaffolding A subunit. Yeast Tap42p and Tip41p are regulators of type 2A phosphatases playing antagonistic roles in the target of rapamycin signaling pathway. a4 and target of rapamycin signaling pathway regulator-like TIPRL are the respective mammalian orthologs of Tap42p and Tip41p. a4 has been characterized as an essential protein implicated in cell signaling differentiation and survival by contrast the role of mammalian TIPRL is still poorly understood. In this study a yeast two-hybrid screen revealed that TIPRL interacts with the C-terminal region of the catalytic subunits of PP2A PP4 and PP6. The TIPRL-interacting region on the catalytic subunit was mapped to residues 210-309 and does not overlap with the a4-binding region as shown by yeast two-hybrid and pull-down assays using recombinant proteins. TIPRL and a4 can bind PP2Ac simultaneously forming a stable ternary .

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