Title: The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations
Authors: Van Hoof, Christine
Janssens, Veerle
De Baere, Ivo
Stark, M J
de Winde, J H
Winderickx, Joris
Thevelein, Johan
Merlevede, Wilfried
Goris, Jozef # ×
Issue Date: Mar-2001
Series Title: Experimental Cell Research vol:264 issue:2 pages:372-87
Abstract: In Saccharomyces cerevisiae, PTPA is encoded by two genes, YPA1 and YPA2. In order to examine the biological role of PTPA as potential regulator of protein phosphatase 2A (PP2A), we compared the phenotypes of the ypaDelta mutants with these of PP2A-deficient strains. While deletion of both YPA genes is lethal, deletion of YPA1 alone results in a phenotype resembling that of PP2A-deficient strains in specific aspects such as aberrant bud morphology, abnormal actin distribution, and similar growth defects under various growth conditions. These phenotypes were even more pronounced when YPA1 was deleted in a pph21Delta genetic background. Moreover, ypaDelta mutants are hypersensitive to nocodazole and show inappropriate mitotic spindle formation as previously described for mutants in the catalytic subunit of PP2A, suggesting that Ypa, like PP2A, has a function in mitotic spindle formation. These results are consistent with an in vivo role of Ypa as a regulator of PP2A. However, unlike a PP2A-deficient strain, ypaDelta mutants do not show a G2 arrest. Therefore, Ypa does not seem to play a role in the regulation of PP2A at this stage of the cell cycle. These results imply that Ypa regulates a specific subset of PP2A functions, possibly by controlling the subunit composition of PP2A.
ISSN: 0014-4827
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
Faculty of Medicine - miscellaneous
Molecular Physiology of Plants and Micro-organisms Section - miscellaneous
Molecular Microbiology and Biotechnology Section - miscellaneous (-)
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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