Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation

Her, Jeng-Horng; Wu, Jie; Rall, T B; Sturgill, Thomas W.; Weber, Michael J.

doi:10.1093/nar/19.13.3743

Cited by 95 publications

(55 citation statements)

References 7 publications

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“…We conclude from this study that the clone we isolated previously [7] encodes a completely functional p42 ''~pk protein: the over-expressed protein encoded by our clone migrates at the molecular weight of 42 kDa in SDS-polyacrylamide gel electrophoresis, elutes at 37% ethylene glycol from a phenyl-Superose column, is tyrosine-phosphorylated in response to growth factors, and is enzymatically active towards the relatively specific substrate myelin basic protein. Finally, the presence of the two signals, tyrosine phosphorylation and enzymatic activity, correlate extremely well after purification (see Figs.…”

Section: Discussionmentioning

confidence: 64%

“…With the ERK1 oligonucleotides we were able to isolate a number of ERKI clones as well as a full-length eDNA corresponding to a candidate p42 ""pk clone. The deduced amino acid sequence of this clone predicted a 42 kDa protein exhibiting the characteristic features of a serine/threonine protein kinase and containing a sequence identical to the site of regulatory phosphorylation we had previously determined for p42 '""pk [5,7].…”

Section: Introductionmentioning

confidence: 82%

“…The corresponding predicted sequence in our p42 "~v~ clone is ARFQPGYRS [7]. The IgG fraction of the antiserum was obtained by protein G chromatography.…”

Section: Febs Letfersmentioning

confidence: 99%

“…p42 ~vk cDNA The full length p42 "~ eDNA was first cloned from a Agtl0 eDNA library into pBlueseript [7]. For transient expression of p42 "~'~ in COS-7 cells, the 1.3 kb H~ndlII/SmaI fragment containing the p42 "~r~ gene was further subcloned i~to pSV2CAT with the ehloramphenicol acetyl transferase (CAT) gene being cut out using/-/indIIl and Hpal restriction enzymes.…”

Section: Construction Of a Vector For Transient Expression Of Recombimentioning

confidence: 99%

“…Since the amino acid sequence surrounding the regulatory phosphorylation sites of p42 '''pk was 85% identical to the equivalent region in ERK1 [5], we used oligonucleotides based on the ERKI sequence to screen a 3T3 eDNA library, with the expectation that a p42 ""pk clone could be obtained [7]. With the ERK1 oligonucleotides we were able to isolate a number of ERKI clones as well as a full-length eDNA corresponding to a candidate p42 ""pk clone.…”

Section: Introductionmentioning

confidence: 99%

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Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein

et al. 1991

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We recently cloned from a mouse 3T3 cell eDNA library a eDNA with sequence similarity to the p42 "~ protein and other members of the MAP kinase family. To determine with certainty which member of the family this clone encodes, we have expressed the eDNA in COS ceils and characterized the protein product. When the pSV2MAP plasmid carrying the full-length clone was transfected into COS cells, a protein of 42 000 Da was expressed. This 42 kDa protein displayed chromatographic properties indistinguishable from the endogenous p42 ""r~, and could be separated from the closely related pp44. In addition, upon serum stimulation, the 42 kDa protein became tyrosine-phosphorylated and enzymatically active towards the substrate myelin basic protein. We conclude that this clone codes for a functional p42 re"p* protein kinase.

show abstract

Section: Discussionmentioning

confidence: 64%

Section: Introductionmentioning

confidence: 82%

“…The corresponding predicted sequence in our p42 "~v~ clone is ARFQPGYRS [7]. The IgG fraction of the antiserum was obtained by protein G chromatography.…”

Section: Febs Letfersmentioning

confidence: 99%

Section: Construction Of a Vector For Transient Expression Of Recombimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein

et al. 1991

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Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein.

1992

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To examine signal transduction events activated by oncogenic p21ras, we have studied kinases that are activated following the scrape loading of p21ras into quiescent cells. We observe rapid activation of 42 kDa and 46 kDa protein kinases. The 42 kDa kinase is the mitogen and extracellular‐signal regulated kinase ERK2, (MAP2 kinase), which is activated by phosphorylation on tyrosine and threonine in response to oncogenic p21ras, while the 46 kDa kinase is likely to be another member of the ERK family. Stimulation of these kinases by oncogenic p21ras does not require the presence of growth factors, showing that oncogenic p21ras uncouples kinase activation from external signals. In ras transformed cell lines, these kinases are constitutively activated. We propose that the kinases are important components of the signal transduction pathway activated by p21ras oncoprotein.

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MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase.

et al. 1992

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A ‘MAP kinase activator’ was purified several thousand‐fold from insulin‐stimulated rabbit skeletal muscle, which resembled the ‘activator’ from nerve growth factor‐stimulated PC12 cells in that it could be inactivated by incubation with protein phosphatase 2A, but not by protein tyrosine phosphatases and its apparent molecular mass was 45–50 kDa. In the presence of MgATP, ‘MAP kinase activator’ converted the normal ‘wild‐type’ 42 kDa MAP kinase from an inactive dephosphorylated form to the fully active diphosphorylated species. Phosphorylation occurred on the same threonine and tyrosine residues which are phosphorylated in vivo in response to growth factors or phorbol esters. A mutant MAP kinase produced by changing a lysine at the active centre to arginine was phosphorylated in an identical manner by the ‘MAP kinase activator’, but no activity was generated. The results demonstrate that ‘MAP kinase activator’ is a protein kinase (MAP kinase kinase) and not a protein that stimulates the autophosphorylation of MAP kinase. MAP kinase kinase is the first established example of a protein kinase that can phosphorylate an exogenous protein on threonine as well as tyrosine residues.

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Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation

Abstract: EMBL accession no. X58712Pp42/MAP kinase (refered to here as p42maPk) becomes

Cited by 95 publications

References 7 publications

Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein

Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein

Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein.

MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase.

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Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation

Abstract: EMBL accession no. X58712Pp42/MAP kinase (refered to here as p42maPk) becomes

Cited by 95 publications

References 7 publications

Functional expression in mammalian cells of a full&#x2010;length cDNA coding for the pp42/MAP kinase (p42mapk) protein

Functional expression in mammalian cells of a full&#x2010;length cDNA coding for the pp42/MAP kinase (p42mapk) protein

Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein.

MAP kinase activator from insulin-stimulated skeletal muscle is a protein threonine/tyrosine kinase.

Contact Info

Product

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Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein

Functional expression in mammalian cells of a full‐length cDNA coding for the pp42/MAP kinase (p42^mapk) protein