Cited by 29Cytokine Signaling Pathways and InteractionsProtein Kinase Regulation and GTPase SignalingProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index; none of the 44 sources its claims cite is checked for support yet.

The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression

Open access

Gündogdu, Mehtap S, Liu, He, Metzdorf, Daniela, Hildebrand, Dagmar, Aigner, Michael, Aktories, Klaus, Heeg, Klaus, Kubatzky, Katharina F·2010·Molecular Cancer

DOI 10.1186/1476-4598-9-225PMC PMC2936343

Open this paper in CoChat — free account Open PDF

Abstract

Background: RhoH is a constitutively active member of the family of Rho GTPases. Its expression is restricted to the haematopoietic lineage, where it serves as a positive regulator for T cell selection and mast cell function and as a negative regulator for growth-related functions in other lineages. Here, we examined the activation of signal transducer and activator of transcription (STAT) proteins in response to stimulation with interleukin 3 (IL3). Results: Using the murine IL3-dependent cell line BaF3 we investigated the influence of RhoH protein expression levels on IL3-mediated cellular responses. RhoH overexpressing cells showed lower sensitivity to IL3 and decreased STAT5 activation. SiRNA-mediated repression of RhoH gene expression led to an increase in proliferation and STAT5 activity which correlated with an increased number of IL3 receptor α chain molecules, also known as CD123, expressed at the cell surface. Interestingly, these findings could be reproduced using human THP-1 cells as a model system for acute myeloid leukaemia, where low RhoH levels are known to be an unfavourable prognostic marker. Overexpression of RhoH on the other hand caused an induction of STAT1 activity and western blot analysis revealed that activated STAT1 is phosphorylated on Tyr701. STAT1 is known to induce apoptosis or cell cycle arrest and we detected an upregulation of cyclin-dependent kinase inhibitors (CDKI) p21 Cip1 and p27 Kip1 in RhoH overexpressing BaF3 cells. Conclusions: We propose that RhoH functions as a negative regulator for IL3-induced signals through modulation of the JAK-STAT pathway. High levels of RhoH allow the IL3-dependent activation of STAT1 causing decreased proliferation through upregulation of p21 Cip1 and p27 Kip1 . Low RhoH levels on the other hand led to an upregulation of IL3-dependent cell growth, STAT5 activity and an increase of CD123 surface expression, linking RhoH to a CD123/STAT5 phenotype that has been described in AML patients.

CoChat Summary

Written by AI from the paper’s full text.

TL;DR

RhoH expression level inversely regulates IL3-driven proliferation in BaF3 cells by modulating STAT1/STAT5 activity and CD123/IRF-1 expression. Low RhoH promotes a STAT5/CD123 phenotype also seen in THP-1 AML cells, while high RhoH activates STAT1 and cell-cycle inhibitors.

Key findings

In BaF3 cells, RhoH overexpression reduced IL3-dependent proliferation to app. 30% of control, whereas siRhoH increased proliferation to 160%; the effect was specific to IL3, as EpoR and EpoR-RhoH cells showed no growth difference.
RhoH overexpression decreased IL3-induced STAT5 phosphorylation to 50% and increased STAT1 Tyr701 phosphorylation app. two-fold; siRhoH increased STAT5 phosphorylation 1.3-fold, with no change in total STAT5 protein.
RhoH overexpression increased p21Cip1 and p27Kip1 mRNA 55- and 40-fold, respectively, and protein levels 2-fold and 1.3-fold; no significant changes were detected in siRhoH cells.
siRhoH BaF3 cells expressed app. 25% more surface CD123 and app. 200-fold higher IRF-1 mRNA, while RhoH overexpression decreased CD123 by app. 50%; in THP-1 cells, RhoH overexpression decreased CD123 by 50% and IRF-1 expression 15-fold.

Methods

Murine IL3-dependent BaF3 proB cells were retrovirally transduced to overexpress RhoH or to express siRhoH, with empty-vector controls; human THP-1 acute monocytic leukaemia cells were transiently transfected with HA-RhoH or vector.
Proliferation/viability was measured by Cell Titer Glo ATP assay, apoptosis by Annexin V/PI FACS, STAT phosphorylation by intracellular FACS and immunoprecipitation/western blot, CD123 surface expression by FACS, and mRNA by quantitative real-time PCR with GAPDH as reference.
Statistical significance was assessed by paired t-test; data are presented as mean ± SD, with most experiments performed at least in three independent experiments, though some quantifications used n = 2.

Limitations

Stated: the exact mechanism by which RhoH negatively regulates Rac1 remains to be elucidated; RhoH-deficient animals showed no obvious haematopoietic defect and did not develop lymphomas, suggesting compensation by other cytokines and a limit of the animal model.
Stated/evident: some supporting data are not shown (IL3-treated bone marrow cells from wildtype vs RhoH-deficient mice; siRhoH survival after cytokine deprivation/readdition), and several experiments have low n (n = 2 for some qPCR/western quantifications).
Evident: the proposed STAT5→IRF-1→CD123 axis is correlative; no direct manipulation of IRF-1 or STAT5 is reported, and THP-1 findings rely on transient transfection.

Model-written summary. Check it against the paper before relying on it.

Integrity signals

Registry

Crossref · 10.1186/1476-4598-9-225

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Figure 1 RhoH regulates IL3-induced proliferation. (A) RhoH mRNA expression levels in control cells, RhoH or siRhoH-transduced BaF3 cells were detected by quantitative real-time PCR using RhoH specific primers and GAPDH as a reference gene. Statistical significance was analysed using the 's t-test (mean ± SD, n = 2 and *P ≤ 0.05; **P ≤ 0.01). (B) FACS analysis of control cells transduced with the empty vector (pMX-IRES-CD4-Puro) or RhoH (pMX-IRES-CD4-Puro RhoH) -transduced BaF3 cells for human CD4 expression after puromycin selection. Parental BaF3 cells were used as a negative control. (C) Dose response curve of control cells, RhoH and siRhoH BaF3 cells cultivated with increasing concentrations of IL3. Viability was determined by quantification of cellular ATP in a Cell Titer Glo assay. Results shown are from one representative experiment performed in triplicates ± SD. (D) Dose response curve of BaF3 cells, BaF3-EpoR cells and BaF3-EpoR cells overexpressing RhoH cultivated with increasing concentrations of Epo. Viability was determined by quantification of cellular ATP in a Cell Titer Glo assay. Results shown are from one representative experiment performed in triplicates ± SD.CC BY · PubMed Central

Figure 2 RhoH expression triggers IL3-dependent STAT1 activation. (A) Control cells, siRhoH and RhoH-transduced BaF3 cells were depleted of cytokine and FBS for 3 h prior to stimulation with IL3. Phosphorylated STAT1 levels were measured with intracellular FACS staining using a FITC-labelled pTyr-STAT1 specific antibody. One representative result of three independent experiments is shown. (B) Control and RhoH cells were starved for 3 hours prior to stimulation with 50 ng/ml IL3. Cells were lysed, STAT1 was immunoprecipitated and tyrosine phosphorylated STAT1 and total STAT1 were detected by enhanced chemiluminescence. Quantification of pSTAT1 levels was done after normalisation to STAT1 levels in cells transduced with the empty vector and is presented as induction of phosphorylation compared to the corresponding unstimulated sample. Statistical significance was analysed using the 's t-test (mean ± SD, n = 3; ***P ≤ 0.005). (D) Apoptosis was induced in control cells, siRhoH or RhoH-transduced cells by cultivation in the absence of IL3 (overnight), treatment with 1 μM staurosporine (3 h) or with 1 μM doxorubicine (12 h) prior to Annexin V/PI staining and FACS analysis (mean ± SD, n = 3).CC BY · PubMed Central

Figure 3 RhoH upregulates p21Cip1 and p27Kip1 expression. (A) Quantification of p21Cip1 and p27Kip1 mRNA expression levels by quantitative SYBR-green PCR in control cells, RhoH and siRhoH-transduced cells. Data were normalised to mRNA levels detected in control cells compared to GAPDH. Statistical significance was analysed using the 's t-test (mean ± SD, n = 3; *P ≤ 0.05). (B, C) Whole cell lysates of control cells, siRhoH and RhoH expressing cells were separated by 4-20% gradient SDS-PAGE and protein expression was detected by antibodies against p21Cip1 and p27Kip1. Protein levels were normalised to β-actin expression (lower panel). Quantification and statistical significance were performed using the 's t-test (mean ± SD, n = 2; *P ≤ 0.05).CC BY · PubMed Central

Figure 4 Low RhoH expression levels enhance STAT5 activity. (A) Control cells, siRhoH and RhoH expressing cells were starved for 3 h in the absence of cytokine and FBS before stimulation with 50 ng/ml IL3. Cells were lysed and STAT5 was immunoprecipitated. Tyrosine phosphorylated STAT5 and total STAT5 were detected by enhanced chemiluminescence using specific antibodies. Quantification of pSTAT5 levels was done after normalisation to total STAT5 levels in control cells and is presented as induction of phosphorylation compared to the corresponding unstimulated sample. Statistical significance was analysed using the 's t-test (mean ± SD, n = 2; *P ≤ 0.05). (B) To verify equal expression levels of STAT5 protein in all cell lines, STAT5 was detected from whole cell lysates and quantified after normalisation to β-actin levels of control cells (mean ± SD, n = 3). (C) pSTAT5 levels were measured by intracellular FACS staining at 0 and 10 min of stimulation of previously starved cells with 50 ng/ml IL3. Representative graphs from one out of three independently performed experiments are shown. (D) CD123 surface expression of control cells, siRhoH and RhoH cells determined by FACS analysis using a CD123-PE antibody. The left panel shows a typical example and the right panel summarises the data of the mean fluorescence signal and the statistical analysis (mean ± SD, n = 3, *P ≤ 0.05). (E) Quantification of IRF-1 mRNA expression levels of control cells and siRhoH-transduced cells was done by quantitative real-time PCR using GAPDH as a reference gene. Data were normalised to the expression in control cells and are presented as fold induction of the IRF-1 gene compared to control cells (mean ± SD, n = 3; *P ≤ 0.05).CC BY · PubMed Central

Figure 5 The AML cell line THP-1 displays an siRhoH phenotype. (A) THP-1 cells were either transfected with HA-RhoH or the empty vector, lysed and separated by SDS-PAGE. Detection of HA-RhoH was performed with an HA-specific antibody and enhanced chemiluminescence. As a loading control, the expression of β-actin was detected. (B) THP-1 cells transfected with HA-RhoH or the empty vector were analysed for CD123 expression by FACS using a CD123-APC antibody. Data are presented as percentage of the mean fluorescence signal for CD123 (mean ± SD, n = 3, *P ≤ 0.05). (C) IRF-1 mRNA expression is decreased in RhoH over-expressing THP-1 cells. Quantification of IRF-1 mRNA expression levels by quantitative SYBR-green PCR in control cells and RhoH-transfected THP-1 cells using human IRF-1 specific primers and GAPDH as a reference gene. Data were normalised to the expression in control cells and are presented as fold induction (mean ± SD, n = 3; ***P ≤ 0.005).CC BY · PubMed Central

Claims the paper makes

38 Own result · 22 Own interpretation · 13 No full text of the sources · 11 Check pending · 9 Own method · 7 Not checked yet

A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“IRF-1 expression was app. 200 fold higher in siRhoH cells compared to control cells”
§ The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > IL3 Receptor α-chain expression is negatively regulated by RhoH
plain
states an association
- Rests on an assumption not shown here.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“RhoH overexpressing cells showed lower sensitivity to IL3 and decreased STAT5 activation.”
- Also stated in: § Underexpression of RhoH enhances STAT5 activity · boosted
  “Western blot analysis (Figure 4A, left panel) and quantification of pSTAT5 levels (Figure 4A, right panel) that was corrected for the level of total STAT5 showed a strong reduction of STAT5 tyrosine phosphorylation compared to control cells (50%).”
§ The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Abstract > Results
boosted
states a cause
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“we found CD123 to be significantly downregulated in RhoH overexpressing cells (50%).”
§ The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > The acute monocytic leukaemia cell line THP-1 displays an siRhoH phenotype
plain
states a cause
- Rests on 2 assumptions not shown here.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“This increased expression was also found in IL3-treated bone marrow cells from wildtype compared to RhoH deficient mice (data not shown).”
§ The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > Overexpression of RhoH leads to the upregulation of p21Cip1 and p27Kip1
plain
states an association
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“siRhoH cells express app. 25% more CD123 than control cells”
§ The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > IL3 Receptor α-chain expression is negatively regulated by RhoH
plain
states a cause
- Rests on 2 assumptions not shown here.

It may state two separate claims as one. 22
Probably not a substantial claim. 34

Create a free account to see these claims.

Create a free account to see these assumptions.

49 more claims

Create a free account to see all 100 claims and to verify the 21 references still open.

See all claims — free account

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

Each contradiction between two passages listed here was confirmed by an independent check.

Rated minor: it would not touch a result — a value no result rests on, a p-value that stays on the same side of the significance level, or a conflict that is clerical, resolved elsewhere in the paper, or outside its own findings.
In the paper
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > RhoH modulates IL3-induced STAT activation
  “(D) Apoptosis was induced in control cells, siRhoH or RhoH-transduced cells by cultivation in the absence of IL3 (overnight), treatment with 1 μM staurosporine (3 h) or with 1 μM doxorubicine (12 h) prior to Annexin V/PI staining and FACS analysis (mean ± SD, n = 3).”
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > RhoH modulates IL3-induced STAT activation
  “However, no difference in the susceptibility of RhoH cells was found compared to control cells (Figure 2C).”
Rated minor: it would not touch a result — a value no result rests on, a p-value that stays on the same side of the significance level, or a conflict that is clerical, resolved elsewhere in the paper, or outside its own findings.
In the paper
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Results > Overexpression of RhoH leads to the upregulation of p21Cip1 and p27Kip1
  “Quantification and statistical significance were performed using the 's t-test (mean ± SD, n = 2; *P ≤ 0.05).”
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Methods > Materials
  “All data shown were performed at least in three independent experiments.”
Rated minor: it would not touch a result — a value no result rests on, a p-value that stays on the same side of the significance level, or a conflict that is clerical, resolved elsewhere in the paper, or outside its own findings.
In the paper
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Background
  “RhoH null mice showed impaired T cell differentiation due to defective T cell receptor signalling [9,16].”
- § The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression > Discussion
  “There was no obvious haematopoietic defect in RhoH-deficient animals, however, it is possible that the disturbed IL3-dependent signalling can be compensated by other cytokines.”

3 of 3

Rho GTPases in cell biology
Etienne-Manneville, S., & Hall, A. (2002) · Nature · doi:10.1038/nature01148 · Cited by 4,201
Targeted Disruption of the Stat1 Gene in Mice Reveals Unexpected Physiologic Specificity in the JAK–STAT Signaling Pathway
Meraz, M. A., White, J. M., Sheehan, K. C. F., Bach, E. A., Rodig, S. J., Dighe, A. S., Kaplan, D. H., Riley, J. K., Greenlund, A. C., Campbell, D., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81288-x · Cited by 1,656
Targeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease
Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,242
Establishment of mouse cell lines which constitutively secrete large quantities of interleukin 2, 3, 4 or 5, using modified cDNA expression vectors
Karasuyama, H., & Melchers, F. (1988) · European Journal of Immunology · doi:10.1002/eji.1830180115 · Cited by 1,059
Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas
Pasqualucci, L., Neumeister, P., Goossens, T., Nanjangud, G., Chaganti, R. S. K., Küppers, R., & Dalla-Favera, R. (2001) · Nature · doi:10.1038/35085588 · Cited by 1,032
Ras and Rho GTPases
Bar‐Sagi, D., & Hall, A. (2000) · Cell · doi:10.1016/s0092-8674(00)00115-x · Cited by 802
Cell Growth Arrest and Induction of Cyclin-Dependent Kinase Inhibitor p21 WAF1/CIP1 Mediated by STAT1
Chin, Y. E., Kitagawa, M., Su, W.-C. S., You, Z.-H., Iwamoto, Y., & Fu, X.-Y. (1996) · Science · doi:10.1126/science.272.5262.719 · Cited by 696
Increasing Complexity of the Ras Signaling Pathway
Vojtek, A. B., & Der, C. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.19925 · Cited by 582
rac, a novel ras-related family of proteins that are botulinum toxin substrates
Didsbury, J., Weber, R. F., Bokoch, G. M., Evans, T., & Snyderman, R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84716-6 · Cited by 575
A novel ras-related gene family
Madaule, P., & Axel, R. (1985) · Cell · doi:10.1016/0092-8674(85)90058-3 · Cited by 502

Show all 38 references

CellFM: a large-scale foundation model pre-trained on transcriptomics of 100 million human cells
Zeng, Y., Xie, J., Shangguan, N., Wei, Z., Li, W., Su, Y., Yang, S., Zhang, C., Zhang, J., Fang, N., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59926-5 · Cited by 120
The role of cytokines in acute myeloid leukemia: A systematic review
Kupsa, T., Horáček, J. M., & Jebavý, L. (2012) · Biomedical Papers · doi:10.5507/bp.2012.108 · Cited by 50
Activation of STAT transcription factors by the Rho-family GTPases
Corry, J., Mott, H. R., & Owen, D. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200468 · Cited by 40
Methanol extract of the ethnopharmaceutical remedy Smilax spinosa exhibits anti-neoplastic activity
Seelinger, M., Popescu, R., Giessrigl, B., Jarukamjorn, K., Unger, C., Wallnöfer, B., Fritzer‐Szekeres, M., Szekeres, T., Díaz, R. E., Jäger, W. R., et al. (2012) · International Journal of Oncology · doi:10.3892/ijo.2012.1538 · Cited by 37
MARCH3 negatively regulates IL-3-triggered inflammatory response by mediating K48-linked polyubiquitination and degradation of IL-3Rα
Feng, L., Li, C., Zeng, L., Gao, D., Sun, Y., Zhong, L., Lin, H., Shu, H., & Li, S. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00834-7 · Cited by 34

See all 29

Signal transduction of the atypical GTPase RhoH in Interleukin-3 dependent cell systems
Gündogdu, M. S. (2011) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00011628
A Role of STAT3 in Rho GTPase-regulated Cell Migration and Proliferation
Debidda, M., Wang, L., Zang, H., Poli, V., & Zheng, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413187200 · Cited by 145
The small GTPase RhoH is an atypical regulator of haematopoietic cells
Fueller, F., & Kubatzky, K. F. (2008) · Cell Communication and Signaling · doi:10.1186/1478-811x-6-6 · Cited by 40
IL-3–induced enhancement of retinoic acid receptor activity is mediated through Stat5, which physically associates with retinoic acid receptors in an IL-3–dependent manner
Si, J., & Collins, S. J. (2002) · Blood · doi:10.1182/blood-2001-12-0374 · Cited by 56
RhoH, a Hematopoietic-Specific Rho Gtpase, Regulates Proliferation, Survival, Migration and Engraftment of Hematopoietic Progenitor Cells.
Gu, Y., Jasti, A. C., Jansen, M., Siefring, J. E., & Lee, K. E. (2004) · Blood · doi:10.1182/blood.v104.11.116.116 · Cited by 4
The R(h)oads to Stat3: Stat3 activation by the Rho GTPases
Raptis, L. H., Arulanandam, R., Geletu, M., & Turkson, J. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.05.008 · Cited by 73
The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient and Modulates Activities of Other Rho GTPases by an Inhibitory Function
Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
Src kinases and not JAKs activate STATs during IL-3 induced myeloid cell proliferation
Chaturvedi, P., Reddy, M. R., & Reddy, E. P. (1998) · Oncogene · doi:10.1038/sj.onc.1201972 · Cited by 145
A GTPase-activating protein binds STAT3 and is required for IL-6–induced STAT3 activation and for differentiation of a leukemic cell line
Tonozuka, Y., Minoshima, Y., Bao, Y. C., Moon, Y., Tsubono, Y., Hatori, T., Nakajima, H., Nosaka, T., Kawashima, T., & Kitamura, T. (2004) · Blood · doi:10.1182/blood-2004-03-1066 · Cited by 44

Authors: Gündogdu, M. S., Liu, H., Metzdorf, D., Hildebrand, D., Aigner, M., Aktories, K., Heeg, K., & Kubatzky, K. F.
Affiliations: Heidelberg University (DE)
University of Bern (CH)
Universitätsklinikum Erlangen (DE)
University of Freiburg (DE)
Corresponding author: Kubatzky, Katharina F
ORCID: Liu, He
Aigner, Michael
Aktories, Klaus
Kubatzky, Katharina F
Venue: Molecular Cancer
Publisher: Springer Science and Business Media LLC
Published: 2010-08-25
Volume: 9
Issue: 1
Pages: 225-225
ISSN: 1476-4598 (ISSN-L)
DOI: 10.1186/1476-4598-9-225
PMC: PMC2936343
OpenAlex: W2148472599
Semantic Scholar: 82c29c1276b025e4a6c8dee1e648fcc5734f17cf
Cited by: 29
References: 38
Citations by year: 2025: 2 · 2024: 4 · 2023: 4 · 2022: 3 · 2021: 1 · 2020: 1 · 2018: 1 · 2016: 2 · 2015: 1 · 2014: 3 · 2013: 1 · 2012: 3
FWCI: 0.90
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Molecular Cancer (publishedVersion, cc-by)
PubMed (publishedVersion)
PubMed Central (publishedVersion, cc-by)
heiDOK (Heidelberg University) (acceptedVersion, other-oa)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: RhoH, Rho GTPases, STAT5, STAT1, CD123, JAK/STAT signaling, acute myeloid leukemia, p21, p27, cell proliferation, hematopoietic cells, Ba/F3 cells, THP-1 cells
MeSH terms: Animals, Cell Line, Interleukin-3, Transcription Factors, Signal Transduction, Up-Regulation, Receptors, Interleukin-3, rho GTP-Binding Proteins, Cell Proliferation, Cyclin-Dependent Kinase Inhibitor p21, Cyclin-Dependent Kinase Inhibitor p27, STAT Transcription Factors, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

A language model drew the claims from the paper on 2026-11-12, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).

A second model labelled each claim on 2026-11-12 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The haematopoietic GTPase RhoH modulates IL3 signalling through regulation of STAT activity and IL3 receptor expression

Abstract

Overview

CoChat Summary

TL;DR

Key findings

Methods

Limitations

Integrity signals

Figures

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks