Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1 (Q28217158)

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6 December 2019

title

Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1 (English)

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6 December 2019

3

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6 December 2019

Melanie H. Cobb

series ordinal

4

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6 December 2019

2

Angelique W Whitehurst

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6 December 2019

author name string

Fred L Robinson

series ordinal

1

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6 December 2019

language of work or name

English

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publication date

31 January 2002

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Journal of Biological Chemistry

6 December 2019

published in

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6 December 2019

volume

277

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6 December 2019

issue

17

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6 December 2019

page(s)

14844-14852

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Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions

6 December 2019

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The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product

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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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Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking

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

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

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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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Protein modification: docking sites for kinases

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Docking domains and substrate-specificity determination for MAP kinases

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Complex formation between RAS and RAF and other protein kinases

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Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity

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MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase

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Crystallization and preliminary X-ray studies of extracellular signal-regulated kinase-2/MAP kinase with an incorporated His-tag

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Mechanism of activation of ERK2 by dual phosphorylation

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Interdependent domains controlling the enzymatic activity of mitogen-activated protein kinase kinase 1.

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Identifiers

DOI

10.1074/JBC.M107776200

2 references

Consolidated OpenCitations Corpus – April 2017

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6 December 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017