Expression and characterization of MAP kinases in bacteria

Charles J. Heise; Melanie H. Cobb

doi:10.1016/j.ymeth.2006.06.012

Expression and characterization of MAP kinases in bacteria

Charles J. Heise, Melanie H. Cobb

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Mitogen-activated protein kinases (MAPKs) are common signal transducers in all eukaryotic organisms. MAPKs are activated by protein kinase cascades consisting of MAPK kinases (MAP2Ks) and MAPK kinase kinases (MAP3Ks). Extracellular-signal regulated kinases 1 and 2 (ERK1/2) are the best characterized MAPKs. Like other MAPKs their activity is regulated by dual phosphorylation as well as dephosphorylation by a host of phosphoprotein phosphatases. The ability to phosphorylate or thiophosphorylate ERK2 in vitro, as described here, is valuable for use in downstream applications designed to investigate MAPK signaling networks.

Original language	English (US)
Pages (from-to)	209-212
Number of pages	4
Journal	Methods
Volume	40
Issue number	3
DOIs	https://doi.org/10.1016/j.ymeth.2006.06.012
State	Published - Nov 2006

Keywords

ERK2
In vitro activation
Phosphorylation
Protein kinase

ASJC Scopus subject areas

Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)

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10.1016/j.ymeth.2006.06.012

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title = "Expression and characterization of MAP kinases in bacteria",

abstract = "Mitogen-activated protein kinases (MAPKs) are common signal transducers in all eukaryotic organisms. MAPKs are activated by protein kinase cascades consisting of MAPK kinases (MAP2Ks) and MAPK kinase kinases (MAP3Ks). Extracellular-signal regulated kinases 1 and 2 (ERK1/2) are the best characterized MAPKs. Like other MAPKs their activity is regulated by dual phosphorylation as well as dephosphorylation by a host of phosphoprotein phosphatases. The ability to phosphorylate or thiophosphorylate ERK2 in vitro, as described here, is valuable for use in downstream applications designed to investigate MAPK signaling networks.",

keywords = "ERK2, In vitro activation, Phosphorylation, Protein kinase",

author = "Heise, {Charles J.} and Cobb, {Melanie H.}",

year = "2006",

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AU - Heise, Charles J.

AU - Cobb, Melanie H.

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AB - Mitogen-activated protein kinases (MAPKs) are common signal transducers in all eukaryotic organisms. MAPKs are activated by protein kinase cascades consisting of MAPK kinases (MAP2Ks) and MAPK kinase kinases (MAP3Ks). Extracellular-signal regulated kinases 1 and 2 (ERK1/2) are the best characterized MAPKs. Like other MAPKs their activity is regulated by dual phosphorylation as well as dephosphorylation by a host of phosphoprotein phosphatases. The ability to phosphorylate or thiophosphorylate ERK2 in vitro, as described here, is valuable for use in downstream applications designed to investigate MAPK signaling networks.

KW - ERK2

KW - In vitro activation

KW - Phosphorylation

KW - Protein kinase

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JO - Methods in Enzymology

JF - Methods in Enzymology

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ER -

Expression and characterization of MAP kinases in bacteria

Abstract

Keywords

ASJC Scopus subject areas

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