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Critical functions of RhoB in support of glioblastoma tumorigenesis.
Ma Y, Gong Y, Cheng Z, Loganathan S, Kao C, Sarkaria JN, Abel TW, Wang J
(2015) Neuro Oncol 17: 516-25
MeSH Terms: Animals, Brain Neoplasms, Cell Proliferation, Cell Survival, Glioblastoma, Humans, Mice, Nude, STAT3 Transcription Factor, Signal Transduction, Tumor Cells, Cultured, Tumor Suppressor Protein p53, rhoB GTP-Binding Protein
Show Abstract · Added January 5, 2016
BACKGROUND - RhoB is a member of the Rho small GTPase family that regulates cytoskeletal dynamics and vesicle trafficking. The RhoB homologs, RhoA and RhoC, have been shown to promote cancer progression and metastasis. In contrast, the functions of RhoB in human cancers are context dependent. Although expression of RhoB inversely correlates with disease progression in several epithelial cancers, recent data suggest that RhoB may support malignant phenotypes in certain cancer types.
METHODS - We assessed RhoB protein levels in glioma surgical specimens and patient-derived xenografts. The roles of RhoB in glioblastoma were determined by loss-of-function and gain-of-function assays in vitro and in vivo. The impact on p53 and STAT3 signaling was investigated.
RESULTS - RhoB expression was similar in tumor specimens compared with normal neural tissues obtained from epilepsy surgery. RhoB was expressed in the vast majority of xenograft tumors and spheroid cultures. Knockdown of RhoB induced cell-cycle arrest and apoptosis and compromised in vivo tumorigenic potential. However, overexpression of wild-type RhoB or a constitutively active mutant (RhoB-V14) did not significantly affect cell growth, which suggests that RhoB is not a rate-limiting oncogenic factor and is consistent with the scarcity of RhoB mutations in human cancer. Knockdown of RhoB reduced basal STAT3 activity and impaired cytokine-induced STAT3 activation. In glioblastoma tumors retaining wild-type p53, depletion of RhoB also activated p53 and induced expression of p21(CIP1) (/WAF1).
CONCLUSIONS - Our data suggest that RhoB belongs to an emerging class of "nononcogene addiction" factors that are essential for maintenance of malignant phenotypes in human cancers.
© The Author(s) 2014. Published by Oxford University Press on behalf of the Society for Neuro-Oncology. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
1 Communities
2 Members
0 Resources
12 MeSH Terms
RhoB plays an essential role in CXCR2 sorting decisions.
Neel NF, Lapierre LA, Goldenring JR, Richmond A
(2007) J Cell Sci 120: 1559-71
MeSH Terms: Actins, Bridged Bicyclo Compounds, Heterocyclic, Cell Line, Chemotaxis, Cycloheximide, Cytochalasin B, Endosomes, Guanosine Triphosphate, Humans, Interleukin-8, Lysosome-Associated Membrane Glycoproteins, Lysosomes, Models, Biological, Mutation, Protein Transport, RNA, Small Interfering, Receptor, IGF Type 2, Receptors, Interleukin-8B, Receptors, Transferrin, Thiazolidines, Transfection, rab GTP-Binding Proteins, rab4 GTP-Binding Proteins, rhoB GTP-Binding Protein
Show Abstract · Added May 30, 2013
The CXCR2 chemokine receptor is a G-protein-coupled receptor that undergoes clathrin-mediated endocytosis upon ligand binding. The trafficking of CXCR2 is crucial for cells to maintain a proper chemotactic response. The mechanisms that regulate the recycling/degradation sorting decision are unknown. In this study, we used dominant-negative (T19N) and GTPase-deficient activated (Q63L) RhoB mutants, as well as RhoB small interfering RNA (siRNA) to investigate the role of RhoB in CXCR2 trafficking. Expression of either of the RhoB mutants or transfection of RhoB siRNA impaired CXCR2-mediated chemotaxis. Expression of RhoB T19N and transfection of RhoB siRNA impaired sorting of CXCR2 to the lysosome after 3 hours of CXCL8 stimulation and impaired CXCL8-induced CXCR2 degradation. In cells expressing the RhoB Q63L mutant, CXCR2 recycling through the Rab11a recycling compartment was impaired after 30 minutes of CXCL8 stimulation as was CXCL8-induced CXCR2 degradation. For cells expressing activated RhoB, CXCR2 colocalized with Rab4, a marker for the rapid recycling pathway, and with the mannose-6-phosphate receptor, which traffics between the trans-Golgi network and endosomes. These data suggest that CXCR2 recycles through alternative pathways. We conclude that oscillation of RhoB GTPase activity is essential for appropriate sorting decisions, and for directing CXCR2 degradation and recycling--events that are required for optimal chemotaxis.
2 Communities
1 Members
0 Resources
24 MeSH Terms
The winged-helix transcription factor Foxd3 suppresses interneuron differentiation and promotes neural crest cell fate.
Dottori M, Gross MK, Labosky P, Goulding M
(2001) Development 128: 4127-38
MeSH Terms: Animals, Avian Proteins, Biomarkers, CD57 Antigens, Cadherins, Cell Differentiation, Cell Movement, Chick Embryo, DNA-Binding Proteins, Embryonic Induction, Forkhead Transcription Factors, Gene Expression Regulation, Developmental, Helix-Turn-Helix Motifs, Mice, Mice, Mutant Strains, Neural Crest, Neurons, PAX3 Transcription Factor, Paired Box Transcription Factors, Repressor Proteins, Snail Family Transcription Factors, Spinal Cord, Trans-Activators, Transcription Factors, rhoB GTP-Binding Protein
Show Abstract · Added June 16, 2011
The neural crest is a migratory cell population that gives rise to multiple cell types in the vertebrate embryo. The intrinsic determinants that segregate neural crest cells from multipotential dorsal progenitors within the neural tube are poorly defined. In this study, we show that the winged helix transcription factor Foxd3 is expressed in both premigratory and migratory neural crest cells. Foxd3 is genetically downstream of Pax3 and is not expressed in regions of Pax3 mutant mice that lack neural crest, implying that Foxd3 may regulate aspects of the neural crest differentiation program. We show that misexpression of Foxd3 in the chick neural tube promotes a neural crest-like phenotype and suppresses interneuron differentiation. Cells that ectopically express Foxd3 upregulate HNK1 and Cad7, delaminate and emigrate from the neural tube at multiple dorsoventral levels. Foxd3 does not induce Slug and RhoB, nor is its ability to promote a neural crest-like phenotype enhanced by co-expression of Slug. Together these results suggest Foxd3 can function independently of Slug and RhoB to promote the development of neural crest cells from neural tube progenitors.
1 Communities
1 Members
0 Resources
25 MeSH Terms
Functional design in the actin cytoskeleton.
Small JV, Rottner K, Kaverina I
(1999) Curr Opin Cell Biol 11: 54-60
MeSH Terms: Actins, Animals, Biological Transport, Cell Adhesion, Cell Line, Cell Movement, Cell Polarity, Cell Size, Cytoskeleton, Dyneins, GTP-Binding Proteins, Kinesin, Membrane Proteins, Microtubules, Models, Biological, Myosins, rac GTP-Binding Proteins, rhoB GTP-Binding Protein
Show Abstract · Added December 10, 2013
Changes in cell shape, anchorage and motility are all associated with the dynamic reorganisation of the architectural arrays of actin filaments that make up the actin cytoskeleton. The relative expression of these functionally different actin filament arrays is intimately linked to the pattern of contacts that a cell develops with its extracellular substrate. Cell polarity is acquired by the development of an asymmetric pattern of substrate contacts, effected in a specific, site-directed manner by the delivery of adhesion-site modulators along microtubules.
0 Communities
1 Members
0 Resources
18 MeSH Terms
RhoB is stabilized by transforming growth factor beta and antagonizes transcriptional activation.
Engel ME, Datta PK, Moses HL
(1998) J Biol Chem 273: 9921-6
MeSH Terms: Animals, Cell Line, GTP Phosphohydrolases, GTP-Binding Proteins, Kinetics, Luciferases, Membrane Proteins, Peptide Hydrolases, Polymerase Chain Reaction, Proteasome Endopeptidase Complex, Protein Prenylation, Recombinant Fusion Proteins, Transcriptional Activation, Transfection, Transforming Growth Factor beta, Ubiquitins, rhoB GTP-Binding Protein
Show Abstract · Added February 17, 2014
Transforming growth factor beta (TGF-beta) is the prototype for an evolutionarily conserved superfamily of secreted factors implicated in diverse biological phenomena. The pleiotropic responses to TGF-beta are initiated by a heteromeric receptor complex that binds and phosphorylates downstream effectors. Among these, the Smads have been extensively studied. However, less attention has been directed toward alternative downstream effectors and their participation in TGF-beta signal transduction. We show that TGF-beta promotes accumulation of the labile monomeric GTPase RhoB by antagonizing its normal proteolytic destruction, presumably via the 26 S proteasome. RhoB accumulates in its isoprenylated form. Transient overexpression of wild type RhoB but not its dominant negative mutant RhoB-N19 antagonizes TGF-beta-mediated transcriptional activation. These results suggest a novel mechanism of regulation by TGF-beta and implicate RhoB as a negative regulator of TGF-beta signal transduction.
0 Communities
1 Members
0 Resources
17 MeSH Terms