Role of non-phosphorylated activation loop residues in determining ERK2 dephosphorylation, activity, and subcellular localization. (Q50675311)

17 March 2018

title

Role of non-phosphorylated activation loop residues in determining ERK2 dephosphorylation, activity, and subcellular localization. (English)

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17 March 2018

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Sarit Bendetz-Nezer

1

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17 March 2018

Rony Seger

series ordinal

2

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17 March 2018

language of work or name

English

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publication date

27 June 2007

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17 March 2018

Journal of Biological Chemistry

number of pages

9

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based on heuristic

inferred from page(s)

published in

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17 March 2018

volume

282

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17 March 2018

issue

34

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17 March 2018

page(s)

25114-25122

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17 March 2018

The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Regulatory mechanisms and functions of MAP kinase signaling pathways.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Mechanisms of MAPK signalling specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

MAPK signal specificity: the right place at the right time

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Extracellular signal-regulated kinase 1c (ERK1c), a novel 42-kilodalton ERK, demonstrates unique modes of regulation, localization, and function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Heterogeneous expression of four MAP kinase isoforms in human tissues

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Protein-protein interactions in the regulation of the extracellular signal-regulated kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Biochemical and biological functions of the N-terminal, noncatalytic domain of extracellular signal-regulated kinase 2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Association of mitogen-activated protein kinase with the microtubule cytoskeleton

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Mitogen-activated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Vimentin binding to phosphorylated Erk sterically hinders enzymatic dephosphorylation of the kinase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Regulation of protein kinases; controlling activity through activation segment conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Nuclear translocation of mitogen-activated protein kinase kinase (MEK1) in response to mitogenic stimulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Induction of the mitogen-activated protein kinase phosphatase MKP3 by nerve growth factor in differentiating PC12

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Non-regulated and stimulated mechanisms cooperate in the nuclear accumulation of MEK1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

A Bipartite Mechanism for ERK2 Recognition by Its Cognate Regulators and Substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

Involvement of the activation loop of ERK in the detachment from cytosolic anchoring

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703120200

21 January 2018

Identifiers

DOI

10.1074/JBC.M703120200

1 reference

17 March 2018

PubMed ID

17597065

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17 March 2018