(Q46847481)

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The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125.

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scholarly article

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125. (English)

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

phosphorylation

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Erika J Mancini

3

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

4

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

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Morag C Martin

1

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Lindsey A Allan

2

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

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publication date

14 December 2007

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

283

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

7

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

3854-3865

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Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

Programmed cell death in animal development

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The protein structures that shape caspase activity, specificity, activation and inhibition

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Regulation of cell death protease caspase-9 by phosphorylation

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Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK.

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Regulation of caspase 9 through phosphorylation by protein kinase C zeta in response to hyperosmotic stress

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Protein kinase A regulates caspase-9 activation by Apaf-1 downstream of cytochrome c.

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ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions

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p38 isoforms have opposite effects on AP-1-dependent transcription through regulation of c-Jun. The determinant roles of the isoforms in the p38 MAPK signal specificity

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A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission

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Docking domains and substrate-specificity determination for MAP kinases

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Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis

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Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1

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Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

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ClusPro: an automated docking and discrimination method for the prediction of protein complexes

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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 novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta

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Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway

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Identification of glycogen synthase as a new substrate for stress-activated protein kinase 2b/p38beta

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BIRB796 inhibits all p38 MAPK isoforms in vitro and in vivo.

1 reference

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

1 reference

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

1 reference

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

1 reference

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Spatially separate docking sites on ERK2 regulate distinct signaling events in vivo

1 reference

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

1 reference

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Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

1 reference

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Specificity determinants in MAPK signaling to transcription factors

1 reference

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An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors

1 reference

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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

1 reference

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Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M705647200

1 reference

Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

25 December 2017

http://europepmc.org/abstract/MED/18083711

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