Docking domains and substrate-specificity determination for MAP kinases (Q34023280)

30 July 2017

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title

Docking domains and substrate-specificity determination for MAP kinases (English)

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30 July 2017

Sharrocks AD

1

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30 July 2017

Yang SH

series ordinal

2

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30 July 2017

Galanis A

series ordinal

3

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30 July 2017

publication date

1 September 2000

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30 July 2017

number of pages

6

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Trends in Biochemical Sciences

inferred from page(s)

published in

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30 July 2017

volume

25

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30 July 2017

issue

9

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30 July 2017

page(s)

448-453

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Mitogen-activated protein kinase pathways

30 July 2017

cites work

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The riddle of MAP kinase signaling specificity

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Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals

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Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain

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The regulation of AP-1 activity by mitogen-activated protein kinases

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Transcription factor ATF2 regulation by the JNK signal transduction pathway

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ATF-2 contains a phosphorylation-dependent transcriptional activation domain

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The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif.

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Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors

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Selective interaction of JNK protein kinase isoforms with transcription factors

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Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1.

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c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions

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ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions

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A cytoplasmic inhibitor of the JNK signal transduction pathway

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PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.

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Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm

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7 January 2021

A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs

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7 January 2021

A conserved docking motif in MAP kinases common to substrates, activators and regulators

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7 January 2021

The N-terminal ERK-binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo

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A MAP kinase docking site is required for phosphorylation and activation of p90(rsk)/MAPKAP kinase-1.

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Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo

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Analysis of the interaction between c-Jun and c-Jun N-terminal kinase in vivo

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7 January 2021

A mammalian scaffold complex that selectively mediates MAP kinase activation

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7 January 2021

Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1

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7 January 2021

An oncogenic mutation uncouples the v-Jun oncoprotein from positive regulation by the SAPK/JNK pathway in vivo

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7 January 2021

A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase

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7 January 2021

JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation

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7 January 2021

Identification of two distinct regions of p38 MAPK required for substrate binding and phosphorylation

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7 January 2021

Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase

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7 January 2021

Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

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7 January 2021

Protein modification: docking sites for kinases

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7 January 2021

10.1016/S0968-0004(00)01627-3

Identifiers

DOI

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30 July 2017

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