Beclin 1

Autores
Molejon, Maria Ines; Ropolo, Alejandro Javier; Vaccaro, Maria Ines
Año de publicación
2012
Idioma
inglés
Tipo de recurso
parte de libro
Estado
versión publicada
Descripción
Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer (1). The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL (2;3). Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity (3,4). The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway (Molejon et al., Sci Rep. 2012; In press).
Fil: Molejon, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
Fil: Ropolo, Alejandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
Fil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
Materia
BECLIN 1
PANCREAS
AUTOPHAGY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/113545
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Beclin 1Molejon, Maria InesRopolo, Alejandro JavierVaccaro, Maria InesBECLIN 1PANCREASAUTOPHAGYhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer (1). The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL (2;3). Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity (3,4). The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway (Molejon et al., Sci Rep. 2012; In press).Fil: Molejon, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; ArgentinaFil: Ropolo, Alejandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; ArgentinaFil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; ArgentinaMichigan Publishing2012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookParthttp://purl.org/coar/resource_type/c_3248info:ar-repo/semantics/parteDeLibroapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/113545Molejon, Maria Ines; Ropolo, Alejandro Javier; Vaccaro, Maria Ines; Beclin 1; Michigan Publishing; 2012; 1-7978-3-642-55086-7CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.pancreapedia.org/molecules/beclin-1info:eu-repo/semantics/altIdentifier/doi/10.3998/panc.2012.16info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:22:41Zoai:ri.conicet.gov.ar:11336/113545instacron: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:34982025-09-10 13:22:41.769CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Beclin 1
title Beclin 1
spellingShingle Beclin 1
Molejon, Maria Ines
BECLIN 1
PANCREAS
AUTOPHAGY
title_short Beclin 1
title_full Beclin 1
title_fullStr Beclin 1
title_full_unstemmed Beclin 1
title_sort Beclin 1
dc.creator.none.fl_str_mv Molejon, Maria Ines
Ropolo, Alejandro Javier
Vaccaro, Maria Ines
author Molejon, Maria Ines
author_facet Molejon, Maria Ines
Ropolo, Alejandro Javier
Vaccaro, Maria Ines
author_role author
author2 Ropolo, Alejandro Javier
Vaccaro, Maria Ines
author2_role author
author
dc.subject.none.fl_str_mv BECLIN 1
PANCREAS
AUTOPHAGY
topic BECLIN 1
PANCREAS
AUTOPHAGY
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer (1). The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL (2;3). Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity (3,4). The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway (Molejon et al., Sci Rep. 2012; In press).
Fil: Molejon, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
Fil: Ropolo, Alejandro Javier. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
Fil: Vaccaro, Maria Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Ciencias Biológicas. Cátedra de Fisiopatología; Argentina
description Beclin 1/ATG6/Vps30 (UniProtKB/Swiss-Prot Q14457) is a 450 amino-acids length protein, with three domains; BH3 (aminoacid 114 to 123), Coiled Coil domain (CCD; aminoacid 144 to 269) and the Evolutionarily Conserved Domain (ECD; aminoacid 244 to 337). BH3 proteins are part of the Bcl-2 family; they are pro-apoptotic damage sensors that play an important role in protecting against cancer (1). The BH3-only domain of Beclin 1 can interact with Bcl-2 and Bcl-XL (2;3). Both cellular and viral Bcl-2 (vBcl-2), or more specifically ER-targeted Bcl-2, inhibit Beclin 1-dependent autophagy by interfering with the Beclin 1-PtdIns 3-kinase interaction (PI3K) and the Beclin 1-associated PI3K activity (3,4). The interaction between Bcl-2 and Beclin 1 is greatly reduced upon starvation, which suggests that the dissociation of Bcl-2 from Beclin1 is important for activating autophagy. We demonstrated that, VMP1 (Vacuole Membrane Protein 1) displaces Bcl-2 from Beclin 1, partitioning Beclin 1 to the autophagic pathway (Molejon et al., Sci Rep. 2012; In press).
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/bookPart
http://purl.org/coar/resource_type/c_3248
info:ar-repo/semantics/parteDeLibro
status_str publishedVersion
format bookPart
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/113545
Molejon, Maria Ines; Ropolo, Alejandro Javier; Vaccaro, Maria Ines; Beclin 1; Michigan Publishing; 2012; 1-7
978-3-642-55086-7
CONICET Digital
CONICET
url http://hdl.handle.net/11336/113545
identifier_str_mv Molejon, Maria Ines; Ropolo, Alejandro Javier; Vaccaro, Maria Ines; Beclin 1; Michigan Publishing; 2012; 1-7
978-3-642-55086-7
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.pancreapedia.org/molecules/beclin-1
info:eu-repo/semantics/altIdentifier/doi/10.3998/panc.2012.16
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Michigan Publishing
publisher.none.fl_str_mv Michigan Publishing
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
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score 12.48226

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