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
Biblioteca Digital (UBA-FCEN)
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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oai_identifier_str paperaa:paper_19326203_v8_n2_p_Gerez
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling 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)
collection 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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