A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1

Gavin, Anne-Claude; Nebreda, Angel R.

doi:10.1016/s0960-9822(99)80120-1

Cited by 158Protein Kinase Regulation and GTPase SignalingMelanoma and MAPK PathwaysProtein Tyrosine Phosphatases

A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1

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Gavin, Anne-Claude, Nebreda, Angel R.·1999·Current Biology

DOI 10.1016/s0960-9822(99)80120-1

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Abstract

Activation of the various mitogen-activated protein (MAP) kinase pathways converts many different extracellular stimuli into specific cellular responses by inducing the phosphorylation of particular groups of substrates. One important determinant for substrate specificity is likely to be the amino-acid sequence surrounding the phosphorylation site; however, these sites overlap significantly between different MAP kinase family members. The idea is now emerging that specific docking sites for protein kinases are involved in the efficient binding and phosphorylation of some substrates [1] [2] [3] [4]. The MAP kinase-activated protein (MAPKAP) kinase p90 rsk contains two kinase domains [5]: the amino-terminal domain (D1) is required for the phosphorylation of exogenous substrates whereas the carboxy-terminal domain (D2) is involved in autophosphorylation. Association between the extracellular signal-regulated kinase (Erk) MAP kinases and p90(rsk) family members has been detected in various cell types including Xenopus oocytes [6] [7] [8], where inactive p90(rsk) is bound to the inactive form of the Erk2- like MAP kinase p42(mpk1). Here, we identify a new MAP kinase docking site located at the carboxyl terminus of p90(rsk). This docking site was required for the efficient phosphorylation and activation of p90(rsk) in vitro and in vivo and was also both necessary and sufficient for the stable and specific association with p42(mpk1). The sequence of the docking site was conserved in other MAPKAP kinases, suggesting that it might represent a new class of interaction motif that facilitates efficient and specific signal transduction by MAP kinases.

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MAPKAPKs form specific complexes with their activating MAPK through short C-terminal docking motifs of less than 20 amino acids.
“MAPKAPKs form specific complexes with their activating enzyme through short (<20 amino acid) C-terminal docking motifs (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]
The C-terminal region of MAPKAPKs mediates binding to the MAPK docking groove on ERK or p38 and is indispensable for MAPKAPK activation in cells.
“This region mediates binding to the MAPK docking groove located on ERK or p38 and this association is indispensable for MAPKAPK activation in cells (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]
MAPKAPKs contain a conserved CaMK-type protein kinase domain and a C-terminal extension that enables activation by ERK, p38, or both.
“MAPKAPKs are MAPK activated protein kinases that are comprised of a conserved calcium/calmodulin-dependent (CaMK)-type protein kinase domain and a C-terminal extension that enables activation by various MAPKs (ERK, p38 or both) (25).”
From Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove (2012) · cites this paper as [25]

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Authors: Gavin, A.-C., & Nebreda, A. R.
Affiliations: European Molecular Biology Laboratory (DE)
ORCID: Gavin, Anne-Claude
Venue: Current Biology
Publisher: Elsevier BV
Published: 1999-03
Volume: 9
Issue: 5
Pages: 281-286
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/s0960-9822(99)80120-1
OpenAlex: W2059986458
Cited by: 158
References: 18
Citations by year: 2023: 3 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 2
FWCI: 6.09
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, 5252 d)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
Archive ouverte UNIGE (University of Geneva) (submittedVersion, other-oa)
Funders: Fonds De La Recherche Scientifique - FNRS
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 › Melanoma and MAPK Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: p90RSK, protein phosphorylation, kinase activation, p42 MAP kinase, C-terminal domain, substrate specificity, MAPK signaling, protein-protein interaction motifs
MeSH terms: MAP-Kinase-Activated Kinase 2, Amino Acid Sequence, Animals, Binding Sites, Enzyme Activation, Humans, Molecular Sequence Data, Phosphorylation, Recombinant Fusion Proteins, Xenopus, Protein Serine-Threonine Kinases, Ribosomal Protein S6 Kinases, Mitogen-Activated Protein Kinase 1, Ribosomal Protein S6 Kinases, 90-kDa, Intracellular Signaling Peptides and Proteins

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A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1

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