Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-157 |
Sentence |
denotes |
Carboxymethylation of the PP2A catalytic subunit in Saccharomyces cerevisiae is required for efficient interaction with the B-type subunits Cdc55p and Rts1p. |
T2 |
158-299 |
Sentence |
denotes |
Protein phosphatase 2A (PP2A) is an essential eukaryotic serine/threonine phosphatase known to play important roles in cell cycle regulation. |
T3 |
300-499 |
Sentence |
denotes |
Association of different B-type targeting subunits with the heterodimeric core (A/C) enzyme is known to be an important mechanism of regulating PP2A activity, substrate specificity, and localization. |
T4 |
500-606 |
Sentence |
denotes |
However, how the binding of these targeting subunits to the A/C heterodimer might be regulated is unknown. |
T5 |
607-822 |
Sentence |
denotes |
We have used the budding yeast Saccharomyces cerevisiae as a model system to investigate the hypothesis that covalent modification of the C subunit (Pph21p/Pph22p) carboxyl terminus modulates PP2A complex formation. |
T6 |
823-849 |
Sentence |
denotes |
Two approaches were taken. |
T7 |
850-980 |
Sentence |
denotes |
First, S. cerevisiae cells were generated whose survival depended on the expression of different carboxyl-terminal Pph21p mutants. |
T8 |
981-1209 |
Sentence |
denotes |
Second, the major S. cerevisiae methyltransferase (Ppm1p) that catalyzes the methylation of the PP2A C subunit carboxyl-terminal leucine was identified, and cells deleted for this methyltransferase were utilized for our studies. |
T9 |
1210-1433 |
Sentence |
denotes |
Our results demonstrate that binding of the yeast B subunit, Cdc55p, to Pph21p was disrupted by either acidic substitution of potential carboxyl-terminal phosphorylation sites on Pph21p or by deletion of the gene for Ppm1p. |
T10 |
1434-1563 |
Sentence |
denotes |
Loss of Cdc55p association was accompanied in each case by a large reduction in binding of the yeast A subunit, Tpd3p, to Pph21p. |
T11 |
1564-1700 |
Sentence |
denotes |
Moreover, decreased Cdc55p and Tpd3p binding invariably resulted in nocodazole sensitivity, a known phenotype of CDC55 or TPD3 deletion. |
T12 |
1701-1810 |
Sentence |
denotes |
Furthermore, loss of methylation also greatly reduced the association of another yeast B-type subunit, Rts1p. |
T13 |
1811-1942 |
Sentence |
denotes |
Thus, methylation of Pph21p is important for formation of PP2A trimeric and dimeric complexes, and consequently, for PP2A function. |
T14 |
1943-2111 |
Sentence |
denotes |
Taken together, our results indicate that methylation and phosphorylation may be mechanisms by which the cell dynamically regulates PP2A complex formation and function. |