Extracellular Signal-Regulated Kinase Regulates RhoA Activation and Tumor Cell Plasticity by Inhibiting Guanine Exchange Factor H1 Activity

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Published inMolecular and Cellular Biology Vol. 33; no. 22; pp. 4526 - 4537
Main Authors von Thun, Anne, Preisinger, Christian, Rath, Oliver, Schwarz, Juliane P., Ward, Chris, Monsefi, Naser, Rodríguez, Javier, Garcia-Munoz, Amaya, Birtwistle, Marc, Bienvenut, Willy, Anderson, Kurt I., Kolch, Walter, von Kriegsheim, Alex
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.11.2013
Taylor & Francis
Subjects
Amino Acid Sequence
Animals
Cell Line, Tumor
Cell Movement
Enzyme Activation
Extracellular Signal-Regulated MAP Kinases - metabolism
HEK293 Cells
Humans
Molecular Sequence Data
Mutation
Neoplasm Invasiveness - genetics
Neoplasm Invasiveness - pathology
Neoplasms - genetics
Neoplasms - metabolism
Neoplasms - pathology
Phosphorylation
Proto-Oncogene Proteins c-fos - metabolism
Rats
Rho Guanine Nucleotide Exchange Factors - chemistry
Rho Guanine Nucleotide Exchange Factors - genetics
Rho Guanine Nucleotide Exchange Factors - metabolism
rhoA GTP-Binding Protein - metabolism
RNA Interference
Signal Transduction
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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList In certain Ras mutant cell lines, the inhibition of extracellular signal-regulated kinase (ERK) signaling increases RhoA activity and inhibits cell motility, which was attributed to a decrease in Fra-1 levels. Here we report a Fra-1-independent augmentation of RhoA signaling during short-term inhibition of ERK signaling. Using mass spectrometry-based proteomics, we identified guanine exchange factor H1 (GEF-H1) as mediating this effect. ERK binds to the Rho exchange factor GEF-H1 and phosphorylates it on S959, causing inhibition of GEF-H1 activity and a consequent decrease in RhoA activity. Knockdown experiments and expression of a nonphosphorylatable S959A GEF-H1 mutant showed that this site is crucial in regulating cell motility and invasiveness. Thus, we identified GEF-H1 as a critical ERK effector that regulates motility, cell morphology, and invasiveness.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
In certain Ras mutant cell lines, the inhibition of extracellular signal-regulated kinase (ERK) signaling increases RhoA activity and inhibits cell motility, which was attributed to a decrease in Fra-1 levels. Here we report a Fra-1-independent augmentation of RhoA signaling during short-term inhibition of ERK signaling. Using mass spectrometry-based proteomics, we identified guanine exchange factor H1 (GEF-H1) as mediating this effect. ERK binds to the Rho exchange factor GEF-H1 and phosphorylates it on S959, causing inhibition of GEF-H1 activity and a consequent decrease in RhoA activity. Knockdown experiments and expression of a nonphosphorylatable S959A GEF-H1 mutant showed that this site is crucial in regulating cell motility and invasiveness. Thus, we identified GEF-H1 as a critical ERK effector that regulates motility, cell morphology, and invasiveness.
Author Kurt I. Anderson
Marc Birtwistle
Chris Ward
Alex von Kriegsheim
Anne von Thun
Naser Monsefi
Christian Preisinger
Willy Bienvenut
Amaya Garcia-Munoz
Juliane P. Schwarz
Oliver Rath
Walter Kolch
Javier Rodríguez
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Snippet Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
In certain Ras mutant cell lines, the inhibition of extracellular signal-regulated kinase (ERK) signaling increases RhoA activity and inhibits cell motility,...
In certain Ras mutant cell lines, the inhibition of extracellular signal-regulated kinase (ERK) signaling increases RhoA activity and inhibits cell motility,...
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SubjectTerms Amino Acid Sequence
Animals
Cell Line, Tumor
Cell Movement
Enzyme Activation
Extracellular Signal-Regulated MAP Kinases - metabolism
HEK293 Cells
Humans
Molecular Sequence Data
Mutation
Neoplasm Invasiveness - genetics
Neoplasm Invasiveness - pathology
Neoplasms - genetics
Neoplasms - metabolism
Neoplasms - pathology
Phosphorylation
Proto-Oncogene Proteins c-fos - metabolism
Rats
Rho Guanine Nucleotide Exchange Factors - chemistry
Rho Guanine Nucleotide Exchange Factors - genetics
Rho Guanine Nucleotide Exchange Factors - metabolism
rhoA GTP-Binding Protein - metabolism
RNA Interference
Signal Transduction
Title Extracellular Signal-Regulated Kinase Regulates RhoA Activation and Tumor Cell Plasticity by Inhibiting Guanine Exchange Factor H1 Activity
URI http://mcb.asm.org/content/33/22/4526.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.00585-13
https://www.ncbi.nlm.nih.gov/pubmed/24043311
https://search.proquest.com/docview/1445911718
https://pubmed.ncbi.nlm.nih.gov/PMC3838172
Volume 33
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