YIL113w encodes a functional dual‐specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae

FEBS Letters

Didmon, Mark P²  MacIsaac, Fiona²  Collister, Michelle²  Keyse, Stephen M²  Stark, Michael J¹  MacDonald, Neil Q³ 

[1]Department of Biochemistry, MSI/Wellcome Trust Biocentre, University of Dundee, Dow Street, Dundee DD1 5EH, UK

[2]Cancer Research UK, Molecular Pharmacology Unit, Biomedical Research Centre, Ninewells Hospital, Dundee DD1 9SY, UK

[3]Cancer Research UK, Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: Signalling;    Dephosphorylation;    Cell integrity;    Stress response;    SDP1;    ERK;    extracellular signal-regulated kinase;    MAPK;    mitogen-activated protein kinase;    MBP;    myelin basic protein;    MKP;    MAPK phosphatase;    ORF;    open reading frame;    PP2A;    protein phosphatase type-2A;    PTP;    protein-tyrosine phosphatase;   

DOI  :  10.1016/S0014-5793(02)03220-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown