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Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae

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Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae. / Palacios, Lorena; Dickinson, Robin J.; Sacristan-Reviriego, Almudena; Didmon, Mark P.; Jose Marin, Maria; Martin, Humberto; Keyse, Stephen M.; Molina, Maria.

In: Journal of Biological Chemistry, Vol. 286, No. 49, 09.12.2011, p. 42037-42050.

Research output: Contribution to journalArticle

Harvard

Palacios, L, Dickinson, RJ, Sacristan-Reviriego, A, Didmon, MP, Jose Marin, M, Martin, H, Keyse, SM & Molina, M 2011, 'Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae' Journal of Biological Chemistry, vol 286, no. 49, pp. 42037-42050.

APA

Palacios, L., Dickinson, R. J., Sacristan-Reviriego, A., Didmon, M. P., Jose Marin, M., Martin, H., Keyse, S. M., & Molina, M. (2011). Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae. Journal of Biological Chemistry, 286(49), 42037-42050doi: 10.1074/jbc.M111.286948

Vancouver

Palacios L, Dickinson RJ, Sacristan-Reviriego A, Didmon MP, Jose Marin M, Martin H et al. Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae. Journal of Biological Chemistry. 2011 Dec 9;286(49):42037-42050.

Author

Palacios, Lorena; Dickinson, Robin J.; Sacristan-Reviriego, Almudena; Didmon, Mark P.; Jose Marin, Maria; Martin, Humberto; Keyse, Stephen M.; Molina, Maria / Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae.

In: Journal of Biological Chemistry, Vol. 286, No. 49, 09.12.2011, p. 42037-42050.

Research output: Contribution to journalArticle

Bibtex - Download

@article{ca96f4934a2244bd833a0ffeb9d7c985,
title = "Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae",
author = "Lorena Palacios and Dickinson, {Robin J.} and Almudena Sacristan-Reviriego and Didmon, {Mark P.} and {Jose Marin}, Maria and Humberto Martin and Keyse, {Stephen M.} and Maria Molina",
year = "2011",
volume = "286",
number = "49",
pages = "42037--42050",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Distinct Docking Mechanisms Mediate Interactions between the Msg5 Phosphatase and Mating or Cell Integrity Mitogen-activated Protein Kinases (MAPKs) in Saccharomyces cerevisiae

A1 - Palacios,Lorena

A1 - Dickinson,Robin J.

A1 - Sacristan-Reviriego,Almudena

A1 - Didmon,Mark P.

A1 - Jose Marin,Maria

A1 - Martin,Humberto

A1 - Keyse,Stephen M.

A1 - Molina,Maria

AU - Palacios,Lorena

AU - Dickinson,Robin J.

AU - Sacristan-Reviriego,Almudena

AU - Didmon,Mark P.

AU - Jose Marin,Maria

AU - Martin,Humberto

AU - Keyse,Stephen M.

AU - Molina,Maria

PY - 2011/12/9

Y1 - 2011/12/9

N2 - <p>MAPK phosphatases (MKPs) are negative regulators of signaling pathways with distinct MAPK substrate specificities. For example, the yeast dual specificity phosphatase Msg5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity pathways, respectively. Like other MAPK-interacting proteins, most MKPs bind MAPKs through specific docking domains. These include D-motifs, which contain basic residues that interact with acidic residues in the common docking (CD) domain of MAPKs. Here we show that Msg5 interacts not only with Fus3, Kss1, and Slt2 but also with the pseudokinase Slt2 paralog Mlp1. Using yeast two-hybrid and in vitro interaction assays, we have identified distinct regions within the N-terminal domain of Msg5 that differentially bind either the MAPKs Fus3 and Kss1 or Slt2 and Mlp1. Whereas a canonical D-site within Msg5 mediates interaction with the CD domains of Fus3 and Kss1, a novel motif ((IYT104)-I-102) within Msg5 is involved in binding to Slt2 and Mlp1. Furthermore, mutation of this site prevents the phosphorylation of Msg5 by Slt2. This motif is conserved in Sdp1, another MKP that dephosphorylates Slt2, as well as in Msg5 orthologs from other yeast species. A region spanning amino acids 274-373 within Slt2 and Mlp1 mediates binding to this Msg5 motif in a CD domain-independent manner. In contrast, Slt2 uses its CD domain to bind to its upstream activator Mkk1. This binding flexibility may allow MAPK pathways to exploit additional regulatory controls in order to provide fine modulation of both pathway activity and specificity.</p>

AB - <p>MAPK phosphatases (MKPs) are negative regulators of signaling pathways with distinct MAPK substrate specificities. For example, the yeast dual specificity phosphatase Msg5 dephosphorylates the Fus3 and Slt2 MAPKs operating in the mating and cell wall integrity pathways, respectively. Like other MAPK-interacting proteins, most MKPs bind MAPKs through specific docking domains. These include D-motifs, which contain basic residues that interact with acidic residues in the common docking (CD) domain of MAPKs. Here we show that Msg5 interacts not only with Fus3, Kss1, and Slt2 but also with the pseudokinase Slt2 paralog Mlp1. Using yeast two-hybrid and in vitro interaction assays, we have identified distinct regions within the N-terminal domain of Msg5 that differentially bind either the MAPKs Fus3 and Kss1 or Slt2 and Mlp1. Whereas a canonical D-site within Msg5 mediates interaction with the CD domains of Fus3 and Kss1, a novel motif ((IYT104)-I-102) within Msg5 is involved in binding to Slt2 and Mlp1. Furthermore, mutation of this site prevents the phosphorylation of Msg5 by Slt2. This motif is conserved in Sdp1, another MKP that dephosphorylates Slt2, as well as in Msg5 orthologs from other yeast species. A region spanning amino acids 274-373 within Slt2 and Mlp1 mediates binding to this Msg5 motif in a CD domain-independent manner. In contrast, Slt2 uses its CD domain to bind to its upstream activator Mkk1. This binding flexibility may allow MAPK pathways to exploit additional regulatory controls in order to provide fine modulation of both pathway activity and specificity.</p>

U2 - 10.1074/jbc.M111.286948

DO - 10.1074/jbc.M111.286948

M1 - Article

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 49

VL - 286

SP - 42037

EP - 42050

ER -

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