The Saccharomyces cerevisiae phosphotyrosyl phosphatase activator proteins are required for a subset of the functions disrupted by protein phosphatase 2A mutations.
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.
Afdeling Biochemie, Departement Geneeskunde, Katholieke Universiteit Leuven, Herestraat 49, Leuven, B-3000, Belgium.
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C
Van Hoof
V
V
Janssens
I
I
De Baere
M J
MJ
Stark
J H
JH
de Winde
J
J
Winderickx
J M
JM
Thevelein
W
W
Merlevede
J
J
Goris
D000199:Actins / Q000378:metabolism; D004789:Enzyme Activation; D016195:G2 Phase; D006918:Hydroxyurea / Q000494:pharmacology; D047908:Intracellular Signaling Peptides and Proteins; D008938:Mitosis / Q000502:physiology; D016296:Mutagenesis; D015739:Nocodazole / Q000494:pharmacology; D019696:Peptidylprolyl Isomerase; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D054648:Protein Phosphatase 2; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism; D011506:Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D029701:Saccharomyces cerevisiae Proteins; D008941:Spindle Apparatus / Q000502:physiology
D000199:Actins; D047908:Intracellular Signaling Peptides and Proteins; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D010749:Phosphoprotein Phosphatases; D054648:Protein Phosphatase 2; D017027:Protein Tyrosine Phosphatases; D019696:Peptidylprolyl Isomerase; C490203:RRD1 protein, S cerevisiae; D015739:Nocodazole; D006918:Hydroxyurea