Cited by 299Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesMelanoma and MAPK Pathways

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Protein Phosphatase 2A Positively Regulates Ras Signaling by Dephosphorylating KSR1 and Raf-1 on Critical 14-3-3 Binding Sites

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Ory, Stéphane, Zhou, Ming, Conrads, Thomas P, Veenstra, Timothy D, Morrison, Deborah K·2003·Current Biology

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Abstract

Background Kinase Suppressor of Ras (KSR) is a conserved component of the Ras pathway that acts as a molecular scaffold to facilitate signal transmission through the MAPK cascade. Although recruitment of KSR1 from the cytosol to the plasma membrane is required for its scaffolding function, the precise mechanism(s) regulating the translocation of KSR1 have not been fully elucidated.Results Using mass spectrometry to analyze the KSR1-scaffolding complex, we identify the serine/threonine protein phosphatase PP2A as a KSR1-associated protein and show that PP2A is a critical regulator of KSR1 activity. We find that the enzymatic core subunits of PP2A (PR65A and catalytic C) constitutively associate with the N-terminal domain of KSR1, whereas binding of the regulatory PR55B subunit is induced by growth factor treatment. Specific inhibition of PP2A activity prevents the growth factor-induced dephosphorylation event involved in the membrane recruitment of KSR1 and blocks the activation of KSR1-associated MEK and ERK. Moreover, we find that PP2A activity is required for activation of the Raf-1 kinase and that both Raf and KSR1 must be dephosphorylated by PP2A on critical regulatory 14-3-3 binding sites for KSR1 to promote MAPK pathway activation.Conclusions These findings identify KSR1 as novel substrate of PP2A and demonstrate the inducible dephosphorylation of KSR1 in response to Ras pathway activation. Further, these results elucidate a common regulatory mechanism for KSR1 and Raf-1 whereby their localization and activity are modulated by the PP2A-mediated dephosphorylation of critical 14-3-3 binding sites.

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Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,927
Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., & Mann, M. (1996) · Nature · doi:10.1038/379466a0 · Cited by 1,674
Organization and regulation of mitogen-activated protein kinase signaling pathways
Garrington, T. P., & Johnson, G. L. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80028-3 · Cited by 1,268
The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
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Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,069
Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
Verhey, K. J., Meyer, D., Deehan, R., Blenis, J., Schnapp, B. J., Rapoport, T. A., & Margolis, B. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.959 · Cited by 609
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Sontag, E., Fedorov, S. A., Kamibayashi, C., Robbins, D. J., Cobb, M. H., & Mumby, M. C. (1993) · Cell · doi:10.1016/0092-8674(93)90533-v · Cited by 510
Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae
Chol, K.-Y., Satterberg, B., Lyons, D. M., & Elion, E. A. (1994) · Cell · doi:10.1016/0092-8674(94)90427-8 · Cited by 502
Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439
Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
Whitmarsh, A. J., & Davis, R. J. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01309-7 · Cited by 387

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BindingDB Entry 50015760: The overview of Mitogen-activated extracellular signal-regulated kinase (MEK)-based dual inhibitor in the treatment of cancers.
BindingDB (2023) · UC San Diego · doi:10.7270/q2dr30fw

Authors: Ory, S., Zhou, M., Conrads, T. P., Veenstra, T. D., & Morrison, D. K.
Affiliations: Frederick National Laboratory for Cancer Research (US)
Science Applications International Corporation (United States) (US)
Corresponding author: Morrison, Deborah K
ORCID: Ory, Stéphane
Zhou, Ming
Conrads, Thomas P
Veenstra, Timothy D
Morrison, Deborah K
Venue: Current Biology
Publisher: Elsevier BV
Published: 2003-08
Volume: 13
Issue: 16
Pages: 1356-1364
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/s0960-9822(03)00535-9
OpenAlex: W2166077873
Cited by: 296
References: 41
Citations by year: 2026: 1 · 2025: 7 · 2024: 8 · 2023: 8 · 2022: 9 · 2021: 9 · 2020: 14 · 2019: 12 · 2018: 10 · 2017: 10 · 2016: 11 · 2015: 9 · 2014: 13 · 2013: 16 · 2012: 12
FWCI: 7.48
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3638 d)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
DigitalCommons-Cedarville (Cedarville University) (submittedVersion)
HAL (submittedVersion)
Funders: U.S. Public Health Service (N01C012400)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords: protein phosphatase 2A, KSR1, Raf-1, Ras signaling, MAPK signaling, dephosphorylation, membrane recruitment, MEK activation, ERK activation, growth factor signaling, scaffold proteins
MeSH terms: Amino Acid Sequence, Animals, Binding Sites, Enzyme Activation, Models, Biological, Molecular Sequence Data, Peptide Fragments, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Recombinant Proteins, Substrate Specificity, Tyrosine 3-Monooxygenase, Signal Transduction, 3T3 Cells, ras Proteins, COS Cells, Proto-Oncogene Proteins c-raf, MAP Kinase Signaling System, 14-3-3 Proteins, Mice, Protein Phosphatase 2, In Vitro Techniques

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Protein Phosphatase 2A Positively Regulates Ras Signaling by Dephosphorylating KSR1 and Raf-1 on Critical 14-3-3 Binding Sites

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