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

Michelle Collister; Mark P. Didmon; Fiona MacIsaac; Michael J. Stark; Neil Q. MacDonald; Stephen M. Keyse

doi:10.1016/S0014-5793(02)03220-9

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

Michelle Collister
, Mark P. Didmon
, Fiona MacIsaac
, Michael J. Stark
, Neil Q. MacDonald
, Stephen M. Keyse

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

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
Pages (from-to)	186-92
Number of pages	7
Journal	FEBS Letters
Volume	527
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03220-9
Publication status	Published - 11 Sept 2002

Keywords

Signalling
DEPHOSPHORYLATION
Cell integrity
Stress response
SDP1

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10.1016/S0014-5793(02)03220-9

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@article{dfd8b0c87e4643428dc64b9b496da316,

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

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.",

keywords = "Signalling, DEPHOSPHORYLATION, Cell integrity, Stress response, SDP1",

author = "Michelle Collister and Didmon, \{Mark P.\} and Fiona MacIsaac and Stark, \{Michael J.\} and MacDonald, \{Neil Q.\} and Keyse, \{Stephen M.\}",

year = "2002",

month = sep,

day = "11",

doi = "10.1016/S0014-5793(02)03220-9",

language = "English",

volume = "527",

pages = "186--92",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley",

number = "1-3",

}

TY - JOUR

T1 - YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae

AU - Collister, Michelle

AU - Didmon, Mark P.

AU - MacIsaac, Fiona

AU - Stark, Michael J.

AU - MacDonald, Neil Q.

AU - Keyse, Stephen M.

PY - 2002/9/11

Y1 - 2002/9/11

N2 - 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.

AB - 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.

KW - Signalling

KW - DEPHOSPHORYLATION

KW - Cell integrity

KW - Stress response

KW - SDP1

U2 - 10.1016/S0014-5793(02)03220-9

DO - 10.1016/S0014-5793(02)03220-9

M3 - Article

C2 - 12220658

SN - 0014-5793

VL - 527

SP - 186

EP - 192

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

Abstract

Keywords

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