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Article

Bacterial Expression, Purification and In Vitro Phosphorylation of Full-Length Ribosomal S6 Kinase 2 (RSK2).

PloS one - 1 Jan 2016

Utepbergenov Darkhan, Hennig Paulina M, Derewenda Urszula, Artamonov Mykhaylo V, Somlyo Avril V, Derewenda Zygmunt S

Abstract excerpt

Ribosomal S6 kinases (RSK) play important roles in cell signaling through the mitogen-activated protein kinase (MAPK) pathway. Each of the four RSK isoforms (RSK1-4) is a single polypeptide chain containing two kinase domains connected by a linker sequence with regulatory phosphorylation sites. Here, we demonstrate that full-length RSK2-which is implicated in several types of cancer, and which is linked to the...

Topics

3-Phosphoinositide-Dependent Protein Kinases
Animals
Cloning, Molecular
Enzyme Activation
Escherichia coli
Humans
Male
Mice
Mice, Inbred C57BL
Mitogen-Activated Protein Kinase 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phosphorylation

Recombinant Fusion Proteins

Ribosomal Protein S6 Kinases, 90-kDa

Source

Open in PubMed Open full text

Identifiers

PMID: 27732676
DOI: 10.1371/journal.pone.0164343
PMCID: PMC5061434

Genes

MBP
PDK1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Bacterial Expression, Purification and In Vitro Phosphorylation of Full-Length Ribosomal S6 Kinase 2 (RSK2).PMID 27732676Read ↗

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