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Article: Roles of USP1 in Ewing sarcoma.

Jayabal, Panneerselvam / Ma, Xiuye / Shiio, Yuzuru

2024 Volume 15, Page(s) 15–27

Abstract: Ewing sarcoma is a cancer of bone and soft tissue in children and young adults that is driven by the EWS-ETS fusion transcription factor, most commonly EWS-FLI1. We previously reported that Ewing sarcoma harbors two populations of cells, the ... ...

Abstract	Ewing sarcoma is a cancer of bone and soft tissue in children and young adults that is driven by the EWS-ETS fusion transcription factor, most commonly EWS-FLI1. We previously reported that Ewing sarcoma harbors two populations of cells, the CD133
Language	English
Publishing date	2024-02-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2538519-7
ISSN	1947-6027 ; 1947-6019
ISSN (online)	1947-6027
ISSN	1947-6019
DOI	10.18632/genesandcancer.235
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Article: EZH2 suppresses endogenous retroviruses and an interferon response in cancers.

Jayabal, Panneerselvam / Ma, Xiuye / Shiio, Yuzuru

Genes & cancer

2021 Volume 12, Page(s) 96–105

Abstract: Ewing sarcoma is an aggressive cancer of bone and soft tissue in children. It is characterized by the chromosomal translocation between EWS and an Ets family transcription factor, most commonly FLI1. We recently reported that Ewing sarcoma depends on the ...

Abstract	Ewing sarcoma is an aggressive cancer of bone and soft tissue in children. It is characterized by the chromosomal translocation between EWS and an Ets family transcription factor, most commonly FLI1. We recently reported that Ewing sarcoma depends on the autocrine signaling mediated by a cytokine, NELL2. NELL2 signaling stimulates the transcriptional output of EWS-FLI1 through the BAF chromatin remodeling complexes. While studying the impact of NELL2 silencing on Ewing sarcoma, we found that suppression of NELL2 signaling induces the expression of endogenous retroviruses (ERVs) and LINE-1 retrotransposons, an interferon response, and growth arrest. We determined that a histone methyltransferase, EZH2, is the critical downstream target of NELL2 signaling in suppressing ERVs, LINE-1, an interferon response, and growth arrest. We show that EZH2 inhibitors induce ERVs, LINE-1, and an interferon response in a variety of cancer types. These results uncover the role for NELL2-EZH2 signaling in suppressing endogenous virus-like agents and an antiviral response, and suggest the potential utility of EZH2 inhibitors in enhancing anti-tumor immunity.
Language	English
Publishing date	2021-12-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	2538519-7
ISSN	1947-6027 ; 1947-6019
ISSN (online)	1947-6027
ISSN	1947-6019
DOI	10.18632/genesandcancer.218
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Article: EWS-FLI-1 creates a cell surface microenvironment conducive to IGF signaling by inducing pappalysin-1.

Jayabal, Panneerselvam / Houghton, Peter J / Shiio, Yuzuru

Genes & cancer

2018 Volume 8, Issue 11-12, Page(s) 762–770

Abstract: Ewing sarcoma is an aggressive cancer of bone and soft tissue in children with poor prognosis. It is characterized by the chromosomal translocation between EWS and an Ets family transcription factor, most commonly FLI-1. EWS-FLI-1 fusion accounts for 85% ...

Abstract	Ewing sarcoma is an aggressive cancer of bone and soft tissue in children with poor prognosis. It is characterized by the chromosomal translocation between EWS and an Ets family transcription factor, most commonly FLI-1. EWS-FLI-1 fusion accounts for 85% of Ewing sarcoma cases. EWS-FLI-1 regulates the expression of a number of genes important for sarcomagenesis, can transform NIH3T3 and C3H10T1/2 cells, and is necessary for proliferation and tumorigenicity of Ewing sarcoma cells, suggesting that EWS-FLI-1 is the causative oncoprotein. Here we report that EWS-FLI-1 induces the expression of pappalysin-1 (PAPPA), a cell surface protease that degrades IGF binding proteins (IGFBPs) and increases the bioavailability of IGF. EWS-FLI-1 binds to the pappalysin-1 gene promoter and stimulates the expression of pappalysin-1, leading to degradation of IGFBPs and enhanced IGF signaling. Silencing of pappalysin-1 strongly inhibited anchorage-dependent and anchorage-independent growth as well as xenograft tumorigenicity of Ewing sarcoma cells. These results suggest that EWS-FLI-1 creates a cell surface microenvironment conducive to IGF signaling by inducing pappalysin-1, which emerged as a novel target to inhibit IGF signaling in Ewing sarcoma.
Language	English
Publishing date	2018-01-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2538519-7
ISSN	1947-6027 ; 1947-6019
ISSN (online)	1947-6027
ISSN	1947-6019
DOI	10.18632/genesandcancer.159
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Article ; Online: Nitric oxide suppression by secreted frizzled-related protein 2 drives retinoblastoma.

Jayabal, Panneerselvam / Zhou, Fuchun / Ma, Xiuye / Bondra, Kathryn M / Blackman, Barron / Weintraub, Susan T / Chen, Yidong / Chévez-Barrios, Patricia / Houghton, Peter J / Gallie, Brenda / Shiio, Yuzuru

Cell reports

2023 Volume 42, Issue 2, Page(s) 112103

Abstract: Retinoblastoma is a cancer of the infant retina primarily driven by loss of the Rb tumor suppressor gene, which is undruggable. Here, we report an autocrine signaling, mediated by secreted frizzled-related protein 2 (SFRP2), which suppresses nitric oxide ...

Abstract	Retinoblastoma is a cancer of the infant retina primarily driven by loss of the Rb tumor suppressor gene, which is undruggable. Here, we report an autocrine signaling, mediated by secreted frizzled-related protein 2 (SFRP2), which suppresses nitric oxide and enables retinoblastoma growth. We show that coxsackievirus and adenovirus receptor (CXADR) is the cell-surface receptor for SFRP2 in retinoblastoma cells; that CXADR functions as a "dependence receptor," transmitting a growth-inhibitory signal in the absence of SFRP2; and that the balance between SFRP2 and CXADR determines nitric oxide production. Accordingly, high SFRP2 RNA expression correlates with high-risk histopathologic features in retinoblastoma. Targeting SFRP2 signaling by SFRP2-binding peptides or by a pharmacological inhibitor rapidly induces nitric oxide and profoundly inhibits retinoblastoma growth in orthotopic xenograft models. These results reveal a cytokine signaling pathway that regulates nitric oxide production and retinoblastoma cell proliferation and is amenable to therapeutic intervention.
MeSH term(s)	Humans ; Nitric Oxide ; Retinal Neoplasms ; Retinoblastoma ; Secreted Frizzled-Related Proteins ; Signal Transduction
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Secreted Frizzled-Related Proteins ; SFRP2 protein, human
Language	English
Publishing date	2023-02-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112103
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Article ; Online: NELL2-cdc42 signaling regulates BAF complexes and Ewing sarcoma cell growth.

Jayabal, Panneerselvam / Zhou, Fuchun / Lei, Xiufen / Ma, Xiuye / Blackman, Barron / Weintraub, Susan T / Houghton, Peter J / Shiio, Yuzuru

Cell reports

2021 Volume 36, Issue 1, Page(s) 109254

Abstract: BAF chromatin remodeling complexes play important roles in chromatin regulation and cancer. Here, we report that Ewing sarcoma cells are dependent on the autocrine signaling mediated by NELL2, a secreted glycoprotein that has been characterized as an ... ...

Abstract	BAF chromatin remodeling complexes play important roles in chromatin regulation and cancer. Here, we report that Ewing sarcoma cells are dependent on the autocrine signaling mediated by NELL2, a secreted glycoprotein that has been characterized as an axon guidance molecule. NELL2 uses Robo3 as the receptor to transmit critical growth signaling. NELL2 signaling inhibits cdc42 and upregulates BAF complexes and EWS-FLI1 transcriptional output. We demonstrate that cdc42 is a negative regulator of BAF complexes, inducing actin polymerization and complex disassembly. Furthermore, we identify NELL2
MeSH term(s)	AC133 Antigen/metabolism ; Actins/metabolism ; Animals ; Cell Line, Tumor ; Cell Proliferation ; Chromatin Assembly and Disassembly ; Down-Regulation ; Gene Expression Regulation, Neoplastic ; Humans ; Mice, SCID ; Multiprotein Complexes/metabolism ; Nerve Tissue Proteins/metabolism ; Oncogene Proteins, Fusion/metabolism ; Phenotype ; Polymerization ; Protein Subunits/metabolism ; Proteomics ; Proto-Oncogene Protein c-fli-1/metabolism ; RNA-Binding Protein EWS/metabolism ; Receptors, Cell Surface/metabolism ; Sarcoma, Ewing/genetics ; Sarcoma, Ewing/metabolism ; Sarcoma, Ewing/pathology ; Signal Transduction ; Up-Regulation ; cdc42 GTP-Binding Protein/metabolism ; Mice
Chemical Substances	AC133 Antigen ; Actins ; EWS-FLI fusion protein ; Multiprotein Complexes ; NELL2 protein, human ; Nerve Tissue Proteins ; Oncogene Proteins, Fusion ; Protein Subunits ; Proto-Oncogene Protein c-fli-1 ; RNA-Binding Protein EWS ; ROBO3 protein, human ; Receptors, Cell Surface ; cdc42 GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2021-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.109254
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Article ; Online: Role of galactose in cellular senescence.

Elzi, David J / Song, Meihua / Shiio, Yuzuru

Experimental gerontology

2016 Volume 73, Page(s) 1–4

Abstract: Cellular senescence has been proposed to play critical roles in tumor suppression and organismal aging, but the molecular mechanism of senescence remains incompletely understood. Here we report that a putative lysosomal carbohydrate efflux transporter, ... ...

Abstract	Cellular senescence has been proposed to play critical roles in tumor suppression and organismal aging, but the molecular mechanism of senescence remains incompletely understood. Here we report that a putative lysosomal carbohydrate efflux transporter, Spinster, induces cellular senescence in human primary fibroblasts. Administration of d-galactose synergistically enhanced Spinster-induced senescence and this synergism required the transporter activity of Spinster. Intracellular d-galactose is metabolized to galactose-1-phosphate by galactokinase. Galactokinase-deficient fibroblasts, which accumulate intracellular d-galactose, displayed increased baseline senescence. Senescence of galactokinase-deficient fibroblasts was further enhanced by d-galactose administration and was diminished by restoration of wild-type galactokinase expression. Silencing galactokinase in normal fibroblasts also induced senescence. These results suggest a role for intracellular galactose in the induction of cellular senescence.
MeSH term(s)	Adaptor Proteins, Signal Transducing/pharmacology ; Adaptor Proteins, Signal Transducing/physiology ; Cells, Cultured ; Cellular Senescence/drug effects ; Cellular Senescence/physiology ; Drug Synergism ; Fibroblasts/cytology ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Galactokinase/deficiency ; Galactokinase/physiology ; Galactose/pharmacology ; Galactose/physiology ; Humans ; Lysosomes/metabolism ; Membrane Proteins/pharmacology ; Membrane Proteins/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; LAT protein, human ; Membrane Proteins ; Galactokinase (EC 2.7.1.6) ; Galactose (X2RN3Q8DNE)
Language	English
Publishing date	2016-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	390992-x
ISSN	1873-6815 ; 0531-5565
ISSN (online)	1873-6815
ISSN	0531-5565
DOI	10.1016/j.exger.2015.11.003
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Zs.A 579: Show issues

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Article ; Online: Redundant Signaling as the Predominant Mechanism for Resistance to Antibodies Targeting the Type-I Insulin-Like Growth Factor Receptor in Cells Derived from Childhood Sarcoma.

Shackleford, Terry J / Hariharan, Seethalakshmi / Vaseva, Angelina V / Alagoa, Karina / Espinoza, Maricruz / Bid, Hemant K / Li, Fuyang / Zhong, Haihong / Phelps, Doris A / Roberts, Ryan D / Cam, Hakan / London, Cheryl A / Guttridge, Denis C / Chen, Yidong / Rao, Manjeet / Shiio, Yuzuru / Houghton, Peter J

Molecular cancer therapeutics

2023 Volume 22, Issue 4, Page(s) 539–550

Abstract: Antibodies targeting insulin-like growth factor 1 receptor (IGF-1R) induce objective responses in only 5% to 15% of children with sarcoma. Understanding the mechanisms of resistance may identify combination therapies that optimize efficacy of IGF-1R- ... ...

Abstract	Antibodies targeting insulin-like growth factor 1 receptor (IGF-1R) induce objective responses in only 5% to 15% of children with sarcoma. Understanding the mechanisms of resistance may identify combination therapies that optimize efficacy of IGF-1R-targeted antibodies. Sensitivity to the IGF-1R-targeting antibody TZ-1 was determined in rhabdomyosarcoma and Ewing sarcoma cell lines. Acquired resistance to TZ-1 was developed and characterized in sensitive Rh41 cells. The BRD4 inhibitor, JQ1, was evaluated as an agent to prevent acquired TZ-1 resistance in Rh41 cells. The phosphorylation status of receptor tyrosine kinases (RTK) was assessed. Sensitivity to TZ-1 in vivo was determined in Rh41 parental and TZ-1-resistant xenografts. Of 20 sarcoma cell lines, only Rh41 was sensitive to TZ-1. Cells intrinsically resistant to TZ-1 expressed multiple (>10) activated RTKs or a relatively less complex set of activated RTKs (∼5). TZ-1 decreased the phosphorylation of IGF-1R but had little effect on other phosphorylated RTKs in all resistant lines. TZ-1 rapidly induced activation of RTKs in Rh41 that was partially abrogated by knockdown of SOX18 and JQ1. Rh41/TZ-1 cells selected for acquired resistance to TZ-1 constitutively expressed multiple activated RTKs. TZ-1 treatment caused complete regressions in Rh41 xenografts and was significantly less effective against the Rh41/TZ-1 xenograft. Intrinsic resistance is a consequence of redundant signaling in pediatric sarcoma cell lines. Acquired resistance in Rh41 cells is associated with rapid induction of multiple RTKs, indicating a dynamic response to IGF-1R blockade and rapid development of resistance. The TZ-1 antibody had greater antitumor activity against Rh41 xenografts compared with other IGF-1R-targeted antibodies tested against this model.
MeSH term(s)	Child ; Humans ; Nuclear Proteins ; Transcription Factors ; Receptor, IGF Type 1 ; Sarcoma/drug therapy ; Receptors, Somatomedin ; Antibodies, Monoclonal/pharmacology ; Cell Line, Tumor ; Cell Cycle Proteins ; SOXF Transcription Factors
Chemical Substances	Nuclear Proteins ; Transcription Factors ; Receptor, IGF Type 1 (EC 2.7.10.1) ; Receptors, Somatomedin ; Antibodies, Monoclonal ; BRD4 protein, human ; Cell Cycle Proteins ; SOX18 protein, human ; SOXF Transcription Factors
Language	English
Publishing date	2023-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2063563-1
ISSN	1538-8514 ; 1535-7163
ISSN (online)	1538-8514
ISSN	1535-7163
DOI	10.1158/1535-7163.MCT-20-0625
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Zs.A 5750: Show issues

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Article ; Online: GDF6-CD99 Signaling Regulates Src and Ewing Sarcoma Growth.

Zhou, Fuchun / Elzi, David J / Jayabal, Panneerselvam / Ma, Xiuye / Chiu, Yu-Chiao / Chen, Yidong / Blackman, Barron / Weintraub, Susan T / Houghton, Peter J / Shiio, Yuzuru

Cell reports

2020 Volume 33, Issue 5, Page(s) 108332

Abstract: We report here that the autocrine signaling mediated by growth and differentiation factor 6 (GDF6), a member of the bone morphogenetic protein (BMP) family of cytokines, maintains Ewing sarcoma growth by preventing Src hyperactivation. Surprisingly, ... ...

Abstract	We report here that the autocrine signaling mediated by growth and differentiation factor 6 (GDF6), a member of the bone morphogenetic protein (BMP) family of cytokines, maintains Ewing sarcoma growth by preventing Src hyperactivation. Surprisingly, Ewing sarcoma depends on the prodomain, not the BMP domain, of GDF6. We demonstrate that the GDF6 prodomain is a ligand for CD99, a transmembrane protein that has been widely used as a marker of Ewing sarcoma. The binding of the GDF6 prodomain to the CD99 extracellular domain results in recruitment of CSK (C-terminal Src kinase) to the YQKKK motif in the intracellular domain of CD99, inhibiting Src activity. GDF6 silencing causes hyperactivation of Src and p21-dependent growth arrest. We demonstrate that two GDF6 prodomain mutants linked to Klippel-Feil syndrome are hyperactive in CD99-Src signaling. These results reveal a cytokine signaling pathway that regulates the CSK-Src axis and cancer cell proliferation and suggest the gain-of-function activity for disease-causing GDF6 mutants.
MeSH term(s)	12E7 Antigen/metabolism ; Animals ; CSK Tyrosine-Protein Kinase/metabolism ; Cell Proliferation ; Down-Regulation ; Gene Expression Regulation, Neoplastic ; Growth Differentiation Factor 6/chemistry ; Growth Differentiation Factor 6/metabolism ; Humans ; Klippel-Feil Syndrome/genetics ; Mice, SCID ; Mutation/genetics ; Oncogene Proteins, Fusion/metabolism ; Protein Domains ; Proteome/metabolism ; Proteomics ; Proto-Oncogene Protein c-fli-1/metabolism ; RNA-Binding Protein EWS/metabolism ; Sarcoma, Ewing/metabolism ; Sarcoma, Ewing/pathology ; Signal Transduction ; Transcription, Genetic ; src-Family Kinases/metabolism
Chemical Substances	12E7 Antigen ; CD99 protein, human ; EWS-FLI fusion protein ; GDF6 protein, human ; Growth Differentiation Factor 6 ; Oncogene Proteins, Fusion ; Proteome ; Proto-Oncogene Protein c-fli-1 ; RNA-Binding Protein EWS ; CSK Tyrosine-Protein Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; CSK protein, human (EC 2.7.10.23)
Language	English
Publishing date	2020-11-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.108332
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Article: Proteomic Analysis of the EWS-Fli-1 Interactome Reveals the Role of the Lysosome in EWS-Fli-1 Turnover

Elzi, DavidJ / Song, Meihua / Hakala, Kevin / Weintraub, Susan T / Shiio, Yuzuru

Journal of Proteome Research. 2014 Aug. 01, v. 13, no. 8

2014

Abstract: Ewing sarcoma is a cancer of bone and soft tissue in children that is characterized by a chromosomal translocation involving EWS and an Ets family transcription factor, most commonly Fli-1. EWS-Fli-1 fusion accounts for 85% of cases. The growth and ... ...

Abstract	Ewing sarcoma is a cancer of bone and soft tissue in children that is characterized by a chromosomal translocation involving EWS and an Ets family transcription factor, most commonly Fli-1. EWS-Fli-1 fusion accounts for 85% of cases. The growth and survival of Ewing sarcoma cells are critically dependent on EWS-Fli-1. A large body of evidence has established that EWS-Fli-1 functions as a DNA-binding transcription factor that regulates the expression of a number of genes important for cell proliferation and transformation. However, little is known about the biochemical properties of the EWS-Fli-1 protein. We undertook a series of proteomic analyses to dissect the EWS-Fli-1 interactome. Employing a proximity-dependent biotinylation technique, BioID, we identified cation-independent mannose 6-phosphate receptor (CIMPR) as a protein located in the vicinity of EWS-Fli-1 within a cell. CIMPR is a cargo that mediates the delivery of lysosomal hydrolases from the trans-Golgi network to the endosome, which are subsequently transferred to the lysosomes. Further molecular cell biological analyses uncovered a role for lysosomes in the turnover of the EWS-Fli-1 protein. We demonstrate that an mTORC1 active-site inhibitor, torin 1, which stimulates the TFEB-lysosome pathway, can induce the degradation of EWS-Fli-1, suggesting a potential therapeutic approach to target EWS-Fli-1 for degradation.
Keywords	active sites ; biotinylation ; cell proliferation ; children ; chromosome translocation ; genes ; hydrolases ; lysosomes ; neoplasm cells ; proteome ; proteomics ; sarcoma ; transcription factors
Language	English
Dates of publication	2014-0801
Size	p. 3783-3791.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021%2Fpr500387m
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 6189: Show issues

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Article ; Online: Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry.

Shiio, Yuzuru / Aebersold, Ruedi

Nature protocols

2006 Volume 1, Issue 1, Page(s) 139–145

Abstract: A main objective of proteomics research is to systematically identify and quantify proteins in a given proteome (cells, subcellular fractions, protein complexes, tissues or body fluids). Protein labeling with isotope-coded affinity tags (ICAT) followed ... ...

Abstract	A main objective of proteomics research is to systematically identify and quantify proteins in a given proteome (cells, subcellular fractions, protein complexes, tissues or body fluids). Protein labeling with isotope-coded affinity tags (ICAT) followed by tandem mass spectrometry allows sequence identification and accurate quantification of proteins in complex mixtures, and has been applied to the analysis of global protein expression changes, protein changes in subcellular fractions, components of protein complexes, protein secretion and body fluids. This protocol describes protein-sample labeling with ICAT reagents, chromatographic fractionation of the ICAT-labeled tryptic peptides, and protein identification and quantification using tandem mass spectrometry. The method is suitable for both large-scale analysis of complex samples including whole proteomes and small-scale analysis of subproteomes, and allows quantitative analysis of proteins, including those that are difficult to analyze by gel-based proteomics technology.
MeSH term(s)	Affinity Labels ; Carbon Isotopes ; Chemical Fractionation/methods ; Deuterium ; Isotope Labeling/methods ; Proteins/analysis ; Proteins/chemistry ; Proteomics/methods ; Tandem Mass Spectrometry
Chemical Substances	Affinity Labels ; Carbon Isotopes ; Proteins ; Deuterium (AR09D82C7G)
Language	English
Publishing date	2006
Publishing country	England
Document type	Journal Article
ZDB-ID	2244966-8
ISSN	1750-2799 ; 1754-2189
ISSN (online)	1750-2799
ISSN	1754-2189
DOI	10.1038/nprot.2006.22
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