Abstract
We show here that the YIL113w gene of Saccharomyces cerevisiae encodes a functional protein phosphatase. Yil113p shows no activity in vitro towards either phosphorylated casein or myelin basic protein. However, Yil113p dephosphorylates activated extracellular signal-regulated kinase 2 MAP kinase indicating that it is a dual-specificity MAP kinase phosphatase. In support of this we find that Yil113p specifically interacts with the stress-activated Slt2/Mpk1p MAP kinase of S. cerevisiae. Furthermore, expression of Yil113p causes the dephosphorylation of Slt2/Mpk1p in vivo, while expression of an inactive mutant of Yil113p causes the accumulation of phosphorylated Slt2/Mpk1p. We conclude that the physiological target of YIL113p is Slt2/Mpk1p.
Original language | English |
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Pages (from-to) | 186-92 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 527 |
Issue number | 1-3 |
DOIs | |
Publication status | Published - 11 Sept 2002 |
Keywords
- Signalling
- DEPHOSPHORYLATION
- Cell integrity
- Stress response
- SDP1