Collister Michelle, Didmon Mark P, MacIsaac Fiona, Stark Michael J, MacDonald Neil Q, Keyse Stephen M
Cancer Research UK, Molecular Pharmacology Unit, Biomedical Research Centre, Ninewells Hospital, DD1 9SY, Dundee, UK
FEBS Lett. 2002 Sep 11;527(1-3):186-92. doi: 10.1016/s0014-5793(02)03220-9.
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.
我们在此表明,酿酒酵母的YIL113w基因编码一种功能性蛋白磷酸酶。Yil113p在体外对磷酸化酪蛋白或髓鞘碱性蛋白均无活性。然而,Yil113p可使活化的细胞外信号调节激酶2丝裂原活化蛋白激酶去磷酸化,表明它是一种双特异性丝裂原活化蛋白激酶磷酸酶。为此我们发现,Yil113p与酿酒酵母的应激激活型Slt2/Mpk1p丝裂原活化蛋白激酶特异性相互作用。此外,Yil113p的表达导致体内Slt2/Mpk1p去磷酸化,而Yil113p无活性突变体的表达导致磷酸化Slt2/Mpk1p的积累。我们得出结论,YIL113p的生理靶点是Slt2/Mpk1p。