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p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta.

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p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta. / Doehn, Ulrik; Gammeltoft, Steen; Shen, Shi-Hsiang; Jensen, Claus J.

I: Biochemical Journal, Bind 382, Nr. Pt 2, 2004, s. 425-31.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Doehn, U, Gammeltoft, S, Shen, S-H & Jensen, CJ 2004, 'p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta.', Biochemical Journal, bind 382, nr. Pt 2, s. 425-31. https://doi.org/10.1042/BJ20040948

APA

Doehn, U., Gammeltoft, S., Shen, S-H., & Jensen, C. J. (2004). p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta. Biochemical Journal, 382(Pt 2), 425-31. https://doi.org/10.1042/BJ20040948

Vancouver

Doehn U, Gammeltoft S, Shen S-H, Jensen CJ. p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta. Biochemical Journal. 2004;382(Pt 2):425-31. https://doi.org/10.1042/BJ20040948

Author

Doehn, Ulrik ; Gammeltoft, Steen ; Shen, Shi-Hsiang ; Jensen, Claus J. / p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta. I: Biochemical Journal. 2004 ; Bind 382, Nr. Pt 2. s. 425-31.

Bibtex

@article{e3bf5090524511dd8d9f000ea68e967b,
title = "p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta.",
abstract = "RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity. Furthermore, PP2Cd is phosphorylated by ERK on Thr315 and Thr333 in the catalytic domain. Mutation of Thr315 and Thr333 to alanine in a catalytically inactive mutant PP2Cdelta (H154D) (His154-->Asp) increases the association with RSK2 significantly, whereas mutation to glutamate, mimicking phosphorylation, reduces the binding of RSK2. The domains of interaction are mapped to the N-terminal extension comprising residues 1-71 of PP2Cd and the N-terminal kinase domain of RSK2. The interaction is specific, since PP2Cd associates with RSK1-RSK4, MSK1 (mitogen- and stress-activated kinase 1) and MSK2, but not with p70 S6 kinase or phosphoinositide-dependent kinase 1. We conclude that RSK2 is associated with PP2Cd in vivo and is partially dephosphorylated by it, leading to reduced kinase activity.",
author = "Ulrik Doehn and Steen Gammeltoft and Shi-Hsiang Shen and Jensen, {Claus J}",
note = "Keywords: Animals; COS Cells; Catalytic Domain; Cell Line; Cercopithecus aethiops; Extracellular Signal-Regulated MAP Kinases; Humans; Kidney; Mutation; Peptides; Phosphoprotein Phosphatases; Phosphorylation; Phosphotransferases; Protein Interaction Mapping; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases; Ribosomal Protein S6 Kinases, 90-kDa",
year = "2004",
doi = "10.1042/BJ20040948",
language = "English",
volume = "382",
pages = "425--31",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cdelta.

AU - Doehn, Ulrik

AU - Gammeltoft, Steen

AU - Shen, Shi-Hsiang

AU - Jensen, Claus J

N1 - Keywords: Animals; COS Cells; Catalytic Domain; Cell Line; Cercopithecus aethiops; Extracellular Signal-Regulated MAP Kinases; Humans; Kidney; Mutation; Peptides; Phosphoprotein Phosphatases; Phosphorylation; Phosphotransferases; Protein Interaction Mapping; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases; Ribosomal Protein S6 Kinases, 90-kDa

PY - 2004

Y1 - 2004

N2 - RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity. Furthermore, PP2Cd is phosphorylated by ERK on Thr315 and Thr333 in the catalytic domain. Mutation of Thr315 and Thr333 to alanine in a catalytically inactive mutant PP2Cdelta (H154D) (His154-->Asp) increases the association with RSK2 significantly, whereas mutation to glutamate, mimicking phosphorylation, reduces the binding of RSK2. The domains of interaction are mapped to the N-terminal extension comprising residues 1-71 of PP2Cd and the N-terminal kinase domain of RSK2. The interaction is specific, since PP2Cd associates with RSK1-RSK4, MSK1 (mitogen- and stress-activated kinase 1) and MSK2, but not with p70 S6 kinase or phosphoinositide-dependent kinase 1. We conclude that RSK2 is associated with PP2Cd in vivo and is partially dephosphorylated by it, leading to reduced kinase activity.

AB - RSK2 (p90 ribosomal S6 kinase 2) is activated via the ERK (extracellular-signal-regulated kinase) pathway by phosphorylation on four sites: Ser227 in the activation loop of the N-terminal kinase domain, Ser369 in the linker, Ser386 in the hydrophobic motif and Thr577 in the C-terminal kinase domain of RSK2. In the present study, we demonstrate that RSK2 is associated in vivo with PP2Cdelta (protein phosphatase 2Cdelta). In epidermal growth factorstimulated cells, RSK2 is partially dephosphorylated on all four sites in an Mn2+-dependent manner, leading to reduced protein kinase activity. Furthermore, PP2Cd is phosphorylated by ERK on Thr315 and Thr333 in the catalytic domain. Mutation of Thr315 and Thr333 to alanine in a catalytically inactive mutant PP2Cdelta (H154D) (His154-->Asp) increases the association with RSK2 significantly, whereas mutation to glutamate, mimicking phosphorylation, reduces the binding of RSK2. The domains of interaction are mapped to the N-terminal extension comprising residues 1-71 of PP2Cd and the N-terminal kinase domain of RSK2. The interaction is specific, since PP2Cd associates with RSK1-RSK4, MSK1 (mitogen- and stress-activated kinase 1) and MSK2, but not with p70 S6 kinase or phosphoinositide-dependent kinase 1. We conclude that RSK2 is associated with PP2Cd in vivo and is partially dephosphorylated by it, leading to reduced kinase activity.

U2 - 10.1042/BJ20040948

DO - 10.1042/BJ20040948

M3 - Journal article

C2 - 15206906

VL - 382

SP - 425

EP - 431

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 2

ER -

ID: 5015411