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Title: An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator
Authors: Longin, Sari ×
Jordens, Jan
Martens, Ellen
Stevens, Ilse
Janssens, Veerle
Rondelez, Evelien
De Baere, Ivo
Derua, Rita
Waelkens, Etienne
Goris, Jozef
Van Hoof, Christine #
Issue Date: May-2004
Publisher: Published by Portland Press on behalf of the Biochemical Society
Series Title: Biochemical Journal vol:380 issue:Pt 1 pages:111-9
Abstract: We have described recently the purification and cloning of PP2A (protein phosphatase 2A) leucine carboxylmethyltransferase. We studied the purification of a PP2A-specific methylesterase that co-purifies with PP2A and found that it is tightly associated with an inactive dimeric or trimeric form of PP2A. These inactive enzyme forms could be reactivated as Ser/Thr phosphatase by PTPA (phosphotyrosyl phosphatase activator of PP2A). PTPA was described previously by our group as a protein that stimulates the in vitro phosphotyrosyl phosphatase activity of PP2A; however, PP2A-specific methyltransferase could not bring about the activation. The PTPA activation could be distinguished from the Mn2+ stimulation observed with some inactive forms of PP2A, also found associated with PME-1 (phosphatase methylesterase 1). We discuss a potential new function for PME-1 as an enzyme that stabilizes an inactivated pool of PP2A.
URI: 
ISSN: 0264-6021
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Department of Materials Engineering - miscellaneous
Faculty of Medicine - miscellaneous
Faculty of Pharmaceutical Sciences - miscellaneous
Laboratory of Phosphoproteomics (-)
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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