The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations

被引:19
作者
Van Hoof, C
Janssens, V
De Baere, I
Stark, MJR
de Winde, JH
Winderickx, J
Thevelein, JM
Merlevede, W
Goris, J
机构
[1] Katholieke Univ Leuven, Dept Geneeskunde, Afdeling Biochem, B-3000 Louvain, Belgium
[2] Univ Dundee, SchLife Sci Bioctr, Dundee DD1 5EH, Scotland
[3] Katholieke Univ Leuven, Lab Mol Celbiol, B-3001 Louvain, Belgium
关键词
phosphotyrosyl phosphatase activator; PTPA; protein phosphatase 2A; PP2A; bud morphology; actin cytoskeleton; cell cycle; mitotic spindle;
D O I
10.1006/excr.2000.5144
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
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 ypa Delta 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 pph21 Delta genetic background. Moreover, ypa Delta 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, ypa Delta mutants do not show a Ga 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 (C) 2001 Academic Press.
引用
收藏
页码:372 / 387
页数:16
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