In Silico Structural and Functional Characterization of the RSUME Splice Variants
- Autores
- Gerez, J.; Fuertes, M.; Tedesco, L.; Silberstein, S.; Sevlever, G.; Paez-Pereda, M.; Holsboer, F.; Turjanski, A.G.; Arzt, E.
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- RSUME (RWD-containing SUMO Enhancer) is a small protein that increases SUMO conjugation to proteins. To date, four splice variants that codify three RSUME isoforms have been described, which differ in their C-terminal end. Comparing the structure of the RSUME isoforms we found that, in addition to the previously described RWD domain in the N-terminal, all these RSUME variants also contain an intermediate domain. Only the longest RSUME isoform presents a C-terminal domain that is absent in the others. Given these differences, we used the shortest and longest RSUME variants for comparative studies. We found that the C-terminal domain is dispensable for the SUMO-conjugation enhancer properties of RSUME. We also demonstrate that these two RSUME variants are equally induced by hypoxia. The NF-κB signaling pathway is inhibited and the HIF-1 pathway is increased more efficiently by the longest RSUME, by means of a greater physical interaction of RSUME267 with the target proteins. In addition, the mRNA and protein levels of these isoforms differ in human glioma samples; while the shortest RSUME isoform is expressed in all the tumors analyzed, the longest variant is expressed in most but not all of them. The results presented here show a degree of redundancy of the RSUME variants on the SUMO pathway. However, the increased inhibition conferred by RSUME267 over the NF-κB signaling pathway, the increased activation over the HIF-1 pathway and the different expression of the RSUME isoforms suggest specific roles for each RSUME isoform which may be relevant in certain types of brain tumors that express RSUME, like human pituitary adenomas and gliomas. © 2013 Gerez et al.
Fil:Gerez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Paez-Pereda, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- PLoS ONE 2013;8(2)
- Materia
-
hypoxia inducible factor 1
immunoglobulin enhancer binding protein
messenger RNA
protein variant
regulator protein
RWD containing SUMO enhancer protein
SUMO protein
unclassified drug
hypoxia inducible factor 1
immunoglobulin enhancer binding protein
isoprotein
RSUME protein, human
SUMO 1 protein
transcription factor
article
brain cancer
carboxy terminal sequence
computer model
controlled study
gene expression
human
human tissue
molecular pathology
molecular weight
nucleotide sequence
protein domain
protein expression
protein function
protein processing
protein protein interaction
regulator gene
RWD containing SUMO enhancer gene
signal transduction
structure activity relation
structure analysis
amino acid sequence
animal
biology
cell line
chemical structure
chemistry
gene expression regulation
genetics
metabolism
molecular genetics
protein secondary structure
Amino Acid Sequence
Animals
Cell Line
Computational Biology
Gene Expression Regulation
Humans
Hypoxia-Inducible Factor 1
Models, Molecular
Molecular Sequence Data
NF-kappa B
Protein Isoforms
Protein Structure, Secondary
Signal Transduction
SUMO-1 Protein
Transcription Factors - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/2.5/ar
- Repositorio
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_19326203_v8_n2_p_Gerez
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In Silico Structural and Functional Characterization of the RSUME Splice VariantsGerez, J.Fuertes, M.Tedesco, L.Silberstein, S.Sevlever, G.Paez-Pereda, M.Holsboer, F.Turjanski, A.G.Arzt, E.hypoxia inducible factor 1immunoglobulin enhancer binding proteinmessenger RNAprotein variantregulator proteinRWD containing SUMO enhancer proteinSUMO proteinunclassified drughypoxia inducible factor 1immunoglobulin enhancer binding proteinisoproteinRSUME protein, humanSUMO 1 proteintranscription factorarticlebrain cancercarboxy terminal sequencecomputer modelcontrolled studygene expressionhumanhuman tissuemolecular pathologymolecular weightnucleotide sequenceprotein domainprotein expressionprotein functionprotein processingprotein protein interactionregulator geneRWD containing SUMO enhancer genesignal transductionstructure activity relationstructure analysisamino acid sequenceanimalbiologycell linechemical structurechemistrygene expression regulationgeneticsmetabolismmolecular geneticsprotein secondary structureAmino Acid SequenceAnimalsCell LineComputational BiologyGene Expression RegulationHumansHypoxia-Inducible Factor 1Models, MolecularMolecular Sequence DataNF-kappa BProtein IsoformsProtein Structure, SecondarySignal TransductionSUMO-1 ProteinTranscription FactorsRSUME (RWD-containing SUMO Enhancer) is a small protein that increases SUMO conjugation to proteins. To date, four splice variants that codify three RSUME isoforms have been described, which differ in their C-terminal end. Comparing the structure of the RSUME isoforms we found that, in addition to the previously described RWD domain in the N-terminal, all these RSUME variants also contain an intermediate domain. Only the longest RSUME isoform presents a C-terminal domain that is absent in the others. Given these differences, we used the shortest and longest RSUME variants for comparative studies. We found that the C-terminal domain is dispensable for the SUMO-conjugation enhancer properties of RSUME. We also demonstrate that these two RSUME variants are equally induced by hypoxia. The NF-κB signaling pathway is inhibited and the HIF-1 pathway is increased more efficiently by the longest RSUME, by means of a greater physical interaction of RSUME267 with the target proteins. In addition, the mRNA and protein levels of these isoforms differ in human glioma samples; while the shortest RSUME isoform is expressed in all the tumors analyzed, the longest variant is expressed in most but not all of them. The results presented here show a degree of redundancy of the RSUME variants on the SUMO pathway. However, the increased inhibition conferred by RSUME267 over the NF-κB signaling pathway, the increased activation over the HIF-1 pathway and the different expression of the RSUME isoforms suggest specific roles for each RSUME isoform which may be relevant in certain types of brain tumors that express RSUME, like human pituitary adenomas and gliomas. © 2013 Gerez et al.Fil:Gerez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Paez-Pereda, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_19326203_v8_n2_p_GerezPLoS ONE 2013;8(2)reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:43:00Zpaperaa:paper_19326203_v8_n2_p_GerezInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:43:01.506Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
title |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
spellingShingle |
In Silico Structural and Functional Characterization of the RSUME Splice Variants Gerez, J. hypoxia inducible factor 1 immunoglobulin enhancer binding protein messenger RNA protein variant regulator protein RWD containing SUMO enhancer protein SUMO protein unclassified drug hypoxia inducible factor 1 immunoglobulin enhancer binding protein isoprotein RSUME protein, human SUMO 1 protein transcription factor article brain cancer carboxy terminal sequence computer model controlled study gene expression human human tissue molecular pathology molecular weight nucleotide sequence protein domain protein expression protein function protein processing protein protein interaction regulator gene RWD containing SUMO enhancer gene signal transduction structure activity relation structure analysis amino acid sequence animal biology cell line chemical structure chemistry gene expression regulation genetics metabolism molecular genetics protein secondary structure Amino Acid Sequence Animals Cell Line Computational Biology Gene Expression Regulation Humans Hypoxia-Inducible Factor 1 Models, Molecular Molecular Sequence Data NF-kappa B Protein Isoforms Protein Structure, Secondary Signal Transduction SUMO-1 Protein Transcription Factors |
title_short |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
title_full |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
title_fullStr |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
title_full_unstemmed |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
title_sort |
In Silico Structural and Functional Characterization of the RSUME Splice Variants |
dc.creator.none.fl_str_mv |
Gerez, J. Fuertes, M. Tedesco, L. Silberstein, S. Sevlever, G. Paez-Pereda, M. Holsboer, F. Turjanski, A.G. Arzt, E. |
author |
Gerez, J. |
author_facet |
Gerez, J. Fuertes, M. Tedesco, L. Silberstein, S. Sevlever, G. Paez-Pereda, M. Holsboer, F. Turjanski, A.G. Arzt, E. |
author_role |
author |
author2 |
Fuertes, M. Tedesco, L. Silberstein, S. Sevlever, G. Paez-Pereda, M. Holsboer, F. Turjanski, A.G. Arzt, E. |
author2_role |
author author author author author author author author |
dc.subject.none.fl_str_mv |
hypoxia inducible factor 1 immunoglobulin enhancer binding protein messenger RNA protein variant regulator protein RWD containing SUMO enhancer protein SUMO protein unclassified drug hypoxia inducible factor 1 immunoglobulin enhancer binding protein isoprotein RSUME protein, human SUMO 1 protein transcription factor article brain cancer carboxy terminal sequence computer model controlled study gene expression human human tissue molecular pathology molecular weight nucleotide sequence protein domain protein expression protein function protein processing protein protein interaction regulator gene RWD containing SUMO enhancer gene signal transduction structure activity relation structure analysis amino acid sequence animal biology cell line chemical structure chemistry gene expression regulation genetics metabolism molecular genetics protein secondary structure Amino Acid Sequence Animals Cell Line Computational Biology Gene Expression Regulation Humans Hypoxia-Inducible Factor 1 Models, Molecular Molecular Sequence Data NF-kappa B Protein Isoforms Protein Structure, Secondary Signal Transduction SUMO-1 Protein Transcription Factors |
topic |
hypoxia inducible factor 1 immunoglobulin enhancer binding protein messenger RNA protein variant regulator protein RWD containing SUMO enhancer protein SUMO protein unclassified drug hypoxia inducible factor 1 immunoglobulin enhancer binding protein isoprotein RSUME protein, human SUMO 1 protein transcription factor article brain cancer carboxy terminal sequence computer model controlled study gene expression human human tissue molecular pathology molecular weight nucleotide sequence protein domain protein expression protein function protein processing protein protein interaction regulator gene RWD containing SUMO enhancer gene signal transduction structure activity relation structure analysis amino acid sequence animal biology cell line chemical structure chemistry gene expression regulation genetics metabolism molecular genetics protein secondary structure Amino Acid Sequence Animals Cell Line Computational Biology Gene Expression Regulation Humans Hypoxia-Inducible Factor 1 Models, Molecular Molecular Sequence Data NF-kappa B Protein Isoforms Protein Structure, Secondary Signal Transduction SUMO-1 Protein Transcription Factors |
dc.description.none.fl_txt_mv |
RSUME (RWD-containing SUMO Enhancer) is a small protein that increases SUMO conjugation to proteins. To date, four splice variants that codify three RSUME isoforms have been described, which differ in their C-terminal end. Comparing the structure of the RSUME isoforms we found that, in addition to the previously described RWD domain in the N-terminal, all these RSUME variants also contain an intermediate domain. Only the longest RSUME isoform presents a C-terminal domain that is absent in the others. Given these differences, we used the shortest and longest RSUME variants for comparative studies. We found that the C-terminal domain is dispensable for the SUMO-conjugation enhancer properties of RSUME. We also demonstrate that these two RSUME variants are equally induced by hypoxia. The NF-κB signaling pathway is inhibited and the HIF-1 pathway is increased more efficiently by the longest RSUME, by means of a greater physical interaction of RSUME267 with the target proteins. In addition, the mRNA and protein levels of these isoforms differ in human glioma samples; while the shortest RSUME isoform is expressed in all the tumors analyzed, the longest variant is expressed in most but not all of them. The results presented here show a degree of redundancy of the RSUME variants on the SUMO pathway. However, the increased inhibition conferred by RSUME267 over the NF-κB signaling pathway, the increased activation over the HIF-1 pathway and the different expression of the RSUME isoforms suggest specific roles for each RSUME isoform which may be relevant in certain types of brain tumors that express RSUME, like human pituitary adenomas and gliomas. © 2013 Gerez et al. Fil:Gerez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Paez-Pereda, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
description |
RSUME (RWD-containing SUMO Enhancer) is a small protein that increases SUMO conjugation to proteins. To date, four splice variants that codify three RSUME isoforms have been described, which differ in their C-terminal end. Comparing the structure of the RSUME isoforms we found that, in addition to the previously described RWD domain in the N-terminal, all these RSUME variants also contain an intermediate domain. Only the longest RSUME isoform presents a C-terminal domain that is absent in the others. Given these differences, we used the shortest and longest RSUME variants for comparative studies. We found that the C-terminal domain is dispensable for the SUMO-conjugation enhancer properties of RSUME. We also demonstrate that these two RSUME variants are equally induced by hypoxia. The NF-κB signaling pathway is inhibited and the HIF-1 pathway is increased more efficiently by the longest RSUME, by means of a greater physical interaction of RSUME267 with the target proteins. In addition, the mRNA and protein levels of these isoforms differ in human glioma samples; while the shortest RSUME isoform is expressed in all the tumors analyzed, the longest variant is expressed in most but not all of them. The results presented here show a degree of redundancy of the RSUME variants on the SUMO pathway. However, the increased inhibition conferred by RSUME267 over the NF-κB signaling pathway, the increased activation over the HIF-1 pathway and the different expression of the RSUME isoforms suggest specific roles for each RSUME isoform which may be relevant in certain types of brain tumors that express RSUME, like human pituitary adenomas and gliomas. © 2013 Gerez et al. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/20.500.12110/paper_19326203_v8_n2_p_Gerez |
url |
http://hdl.handle.net/20.500.12110/paper_19326203_v8_n2_p_Gerez |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/ar |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
PLoS ONE 2013;8(2) reponame:Biblioteca Digital (UBA-FCEN) instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
reponame_str |
Biblioteca Digital (UBA-FCEN) |
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Biblioteca Digital (UBA-FCEN) |
instname_str |
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
instacron_str |
UBA-FCEN |
institution |
UBA-FCEN |
repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
repository.mail.fl_str_mv |
ana@bl.fcen.uba.ar |
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