Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation

Autores
Goitea, Victor Enrique; Hallak, Marta Elena
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT stability, we examined the metabolic fates and degradation mechanisms of cytoplasmic CRT and R-CRT in NIH 3T3 and CHO cells. Both CRT isoforms were found to be proteasomal substrates, but the half-life of R-CRT (2 h) was longer than that of cytoplasmic CRT (0.7 h). Arginylation was not required for proteasomal degradation of CRT, although R-CRT displays ubiquitin modification. A CRT mutant incapable of dimerization showed reduced metabolic stability of R-CRT, indicating that R-CRT dimerization may protect it from proteasomal degradation. Our findings, taken together, demonstrate a novel function of arginylation: increasing the half-life of CRT in cytoplasm.
Fil: Goitea, Victor Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Fil: Hallak, Marta Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Materia
ARGINYLATION
CALRETICULIN
PROTEASOME
PROTEIN DEGRADATION
PROTEIN TURNOVER
DIMER
POST-TRANSLATIONAL MODIFICATION
UBIQUITYLATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10587
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/10587
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal DegradationGoitea, Victor EnriqueHallak, Marta ElenaARGINYLATIONCALRETICULINPROTEASOMEPROTEIN DEGRADATIONPROTEIN TURNOVERDIMERPOST-TRANSLATIONAL MODIFICATIONUBIQUITYLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT stability, we examined the metabolic fates and degradation mechanisms of cytoplasmic CRT and R-CRT in NIH 3T3 and CHO cells. Both CRT isoforms were found to be proteasomal substrates, but the half-life of R-CRT (2 h) was longer than that of cytoplasmic CRT (0.7 h). Arginylation was not required for proteasomal degradation of CRT, although R-CRT displays ubiquitin modification. A CRT mutant incapable of dimerization showed reduced metabolic stability of R-CRT, indicating that R-CRT dimerization may protect it from proteasomal degradation. Our findings, taken together, demonstrate a novel function of arginylation: increasing the half-life of CRT in cytoplasm.Fil: Goitea, Victor Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; ArgentinaFil: Hallak, Marta Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; ArgentinaAmerican Society For Biochemistry And Molecular Biology2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10587Goitea, Victor Enrique; Hallak, Marta Elena; Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation; American Society For Biochemistry And Molecular Biology; Journal of Biological Chemistry; 290; 26; 6-2015; 16403-164140021-92581083-351Xenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/290/26/16403info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M114.626127info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:39Zoai:ri.conicet.gov.ar:11336/10587instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:01:39.635CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
title Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
spellingShingle Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
Goitea, Victor Enrique
ARGINYLATION
CALRETICULIN
PROTEASOME
PROTEIN DEGRADATION
PROTEIN TURNOVER
DIMER
POST-TRANSLATIONAL MODIFICATION
UBIQUITYLATION
title_short Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
title_full Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
title_fullStr Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
title_full_unstemmed Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
title_sort Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
dc.creator.none.fl_str_mv Goitea, Victor Enrique
Hallak, Marta Elena
author Goitea, Victor Enrique
author_facet Goitea, Victor Enrique
Hallak, Marta Elena
author_role author
author2 Hallak, Marta Elena
author2_role author
dc.subject.none.fl_str_mv ARGINYLATION
CALRETICULIN
PROTEASOME
PROTEIN DEGRADATION
PROTEIN TURNOVER
DIMER
POST-TRANSLATIONAL MODIFICATION
UBIQUITYLATION
topic ARGINYLATION
CALRETICULIN
PROTEASOME
PROTEIN DEGRADATION
PROTEIN TURNOVER
DIMER
POST-TRANSLATIONAL MODIFICATION
UBIQUITYLATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT stability, we examined the metabolic fates and degradation mechanisms of cytoplasmic CRT and R-CRT in NIH 3T3 and CHO cells. Both CRT isoforms were found to be proteasomal substrates, but the half-life of R-CRT (2 h) was longer than that of cytoplasmic CRT (0.7 h). Arginylation was not required for proteasomal degradation of CRT, although R-CRT displays ubiquitin modification. A CRT mutant incapable of dimerization showed reduced metabolic stability of R-CRT, indicating that R-CRT dimerization may protect it from proteasomal degradation. Our findings, taken together, demonstrate a novel function of arginylation: increasing the half-life of CRT in cytoplasm.
Fil: Goitea, Victor Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
Fil: Hallak, Marta Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Química Biológica de Córdoba (p); Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
description Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT stability, we examined the metabolic fates and degradation mechanisms of cytoplasmic CRT and R-CRT in NIH 3T3 and CHO cells. Both CRT isoforms were found to be proteasomal substrates, but the half-life of R-CRT (2 h) was longer than that of cytoplasmic CRT (0.7 h). Arginylation was not required for proteasomal degradation of CRT, although R-CRT displays ubiquitin modification. A CRT mutant incapable of dimerization showed reduced metabolic stability of R-CRT, indicating that R-CRT dimerization may protect it from proteasomal degradation. Our findings, taken together, demonstrate a novel function of arginylation: increasing the half-life of CRT in cytoplasm.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
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/11336/10587
Goitea, Victor Enrique; Hallak, Marta Elena; Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation; American Society For Biochemistry And Molecular Biology; Journal of Biological Chemistry; 290; 26; 6-2015; 16403-16414
0021-9258
1083-351X
url http://hdl.handle.net/11336/10587
identifier_str_mv Goitea, Victor Enrique; Hallak, Marta Elena; Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation; American Society For Biochemistry And Molecular Biology; Journal of Biological Chemistry; 290; 26; 6-2015; 16403-16414
0021-9258
1083-351X
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/290/26/16403
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M114.626127
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269709497532416
score 13.13397

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