Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pgen.0030218
Title: A RNA Interference Screen Identifies the Protein Phosphatase 2A Subunit PR55γ as a Stress-Sensitive Inhibitor of c-SRC
Authors: Eichhorn P.J.A. 
Creyghton M.P.
Wilhelmsen K.
Van Dam H.
Bernards R.
Keywords: mitogen activated protein kinase
phosphoprotein phosphatase inhibitor
pr 55 delta
pr55 gamma
serine
unclassified drug
CSK protein, human
oncoprotein
phosphoprotein phosphatase 2
PPP2R2C protein, human
primer DNA
protein tyrosine kinase
stress activated protein kinase
article
drug inhibition
enzyme activity
gene control
gene repression
human
oncogene
phosphorylation
protein analysis
protein protein interaction
RNA interference
ultraviolet irradiation
amino acid substitution
apoptosis
cell line
chemistry
drug antagonism
enzyme activation
genetic transfection
genetics
metabolism
nucleotide sequence
physiology
radiation exposure
signal transduction
site directed mutagenesis
ultraviolet radiation
Amino Acid Substitution
Apoptosis
Base Sequence
Cell Line
DNA Primers
Enzyme Activation
Humans
JNK Mitogen-Activated Protein Kinases
Mutagenesis, Site-Directed
Phosphorylation
Protein Phosphatase 2
Protein-Tyrosine Kinases
Proto-Oncogene Proteins
RNA Interference
Serine
Signal Transduction
Transfection
Ultraviolet Rays
Issue Date: 2007
Publisher: Public Library of Science
Citation: Eichhorn P.J.A., Creyghton M.P., Wilhelmsen K., Van Dam H., Bernards R. (2007). A RNA Interference Screen Identifies the Protein Phosphatase 2A Subunit PR55γ as a Stress-Sensitive Inhibitor of c-SRC. PLoS Genetics 3 (12) : 2381-2394. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pgen.0030218
Abstract: Protein Phosphatase type 2A (PP2A) represents a family of holoenzyme complexes with diverse biological activities. Specific holoenzyme complexes are thought to be deregulated during oncogenic transformation and oncogene-induced signaling. Since most studies on the role of this phosphatase family have relied on the use of generic PP2A inhibitors, the contribution of individual PP2A holoenzyme complexes in PP2A-controlled signaling pathways is largely unclear. To gain insight into this, we have constructed a set of shRNA vectors targeting the individual PP2A regulatory subunits for suppression by RNA interference. Here, we identify PR55γ and PR55δ as inhibitors of c-Jun NH2-terminal kinase (JNK) activation by UV irradiation. We show that PR55γ binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC. We also find that the physical interaction between PR55γ and c-SRC is sensitive to UV irradiation. Our data reveal a novel mechanism of c-SRC regulation whereby in response to stress c-SRC activity is regulated, at least in part, through loss of the interaction with its inhibitor, PR55γ. © 2007 Eichhorn et al.
Source Title: PLoS Genetics
URI: https://scholarbank.nus.edu.sg/handle/10635/165612
ISSN: 15537390
DOI: 10.1371/journal.pgen.0030218
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