FKBP8, a new member of the PIK3C3/VPS34 complex
- Autores
- Aguilera, Milton Osmar; Colombo, Maria Isabel
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Macroautophagy/autophagy is an adaptable pathway involved in the degrada- tion of very different targets that include proteins, organelles, or even invading intracellular microorganisms. The regulation of this complex pathway depends on a great number of proteins, some common for the majority of the processes and others specific for a particular autophagic event. Nevertheless, the kind of interaction between the players contributes to determining the specificity of the regulation. In a recent study, we found a new regulatory protein of starva- tion-activated autophagy called FKBP8. The absence of this protein impairs autophagy activation produced by serum starvation and its overexpression can activate the pathway in cells incubated in full media. Besides, we found that the FKBP8 function is mediated by the interaction with the PIK3C3/VPS34- containing complex. Previously, FKBP8 has been shown to participate in mito- phagy. In the latter process, FKBP8 works inducing mitochondrial fission, and also it functions as a receptor protein through its LIR domain to direct autop- hagy. In contrast to mitophagy, in starvation-activated autophagy, not the LIR but the transmembrane domain of FKBP8 is necessary for the regulatory func- tion and interaction with the PIK3C3 complex.
Fil: Aguilera, Milton Osmar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; Argentina
Fil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; Argentina - Materia
-
FKBP8
AUTOPHAGY
BECLIN1 - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/204333
Ver los metadatos del registro completo
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FKBP8, a new member of the PIK3C3/VPS34 complexAguilera, Milton OsmarColombo, Maria IsabelFKBP8AUTOPHAGYBECLIN1https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Macroautophagy/autophagy is an adaptable pathway involved in the degrada- tion of very different targets that include proteins, organelles, or even invading intracellular microorganisms. The regulation of this complex pathway depends on a great number of proteins, some common for the majority of the processes and others specific for a particular autophagic event. Nevertheless, the kind of interaction between the players contributes to determining the specificity of the regulation. In a recent study, we found a new regulatory protein of starva- tion-activated autophagy called FKBP8. The absence of this protein impairs autophagy activation produced by serum starvation and its overexpression can activate the pathway in cells incubated in full media. Besides, we found that the FKBP8 function is mediated by the interaction with the PIK3C3/VPS34- containing complex. Previously, FKBP8 has been shown to participate in mito- phagy. In the latter process, FKBP8 works inducing mitochondrial fission, and also it functions as a receptor protein through its LIR domain to direct autop- hagy. In contrast to mitophagy, in starvation-activated autophagy, not the LIR but the transmembrane domain of FKBP8 is necessary for the regulatory func- tion and interaction with the PIK3C3 complex.Fil: Aguilera, Milton Osmar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; ArgentinaFil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; ArgentinaTaylor & Francis2022-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/204333Aguilera, Milton Osmar; Colombo, Maria Isabel; FKBP8, a new member of the PIK3C3/VPS34 complex; Taylor & Francis; Autophagy Reports; 8; 7-2022; 291-2942769-4127CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/27694127.2022.2100041info:eu-repo/semantics/altIdentifier/doi/10.1080/27694127.2022.2100041info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:43:51Zoai:ri.conicet.gov.ar:11336/204333instacron: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:34982025-09-29 10:43:52.005CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
FKBP8, a new member of the PIK3C3/VPS34 complex |
title |
FKBP8, a new member of the PIK3C3/VPS34 complex |
spellingShingle |
FKBP8, a new member of the PIK3C3/VPS34 complex Aguilera, Milton Osmar FKBP8 AUTOPHAGY BECLIN1 |
title_short |
FKBP8, a new member of the PIK3C3/VPS34 complex |
title_full |
FKBP8, a new member of the PIK3C3/VPS34 complex |
title_fullStr |
FKBP8, a new member of the PIK3C3/VPS34 complex |
title_full_unstemmed |
FKBP8, a new member of the PIK3C3/VPS34 complex |
title_sort |
FKBP8, a new member of the PIK3C3/VPS34 complex |
dc.creator.none.fl_str_mv |
Aguilera, Milton Osmar Colombo, Maria Isabel |
author |
Aguilera, Milton Osmar |
author_facet |
Aguilera, Milton Osmar Colombo, Maria Isabel |
author_role |
author |
author2 |
Colombo, Maria Isabel |
author2_role |
author |
dc.subject.none.fl_str_mv |
FKBP8 AUTOPHAGY BECLIN1 |
topic |
FKBP8 AUTOPHAGY BECLIN1 |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Macroautophagy/autophagy is an adaptable pathway involved in the degrada- tion of very different targets that include proteins, organelles, or even invading intracellular microorganisms. The regulation of this complex pathway depends on a great number of proteins, some common for the majority of the processes and others specific for a particular autophagic event. Nevertheless, the kind of interaction between the players contributes to determining the specificity of the regulation. In a recent study, we found a new regulatory protein of starva- tion-activated autophagy called FKBP8. The absence of this protein impairs autophagy activation produced by serum starvation and its overexpression can activate the pathway in cells incubated in full media. Besides, we found that the FKBP8 function is mediated by the interaction with the PIK3C3/VPS34- containing complex. Previously, FKBP8 has been shown to participate in mito- phagy. In the latter process, FKBP8 works inducing mitochondrial fission, and also it functions as a receptor protein through its LIR domain to direct autop- hagy. In contrast to mitophagy, in starvation-activated autophagy, not the LIR but the transmembrane domain of FKBP8 is necessary for the regulatory func- tion and interaction with the PIK3C3 complex. Fil: Aguilera, Milton Osmar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; Argentina Fil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto Histología y Embriología D/mend Dr.m.burgos; Argentina |
description |
Macroautophagy/autophagy is an adaptable pathway involved in the degrada- tion of very different targets that include proteins, organelles, or even invading intracellular microorganisms. The regulation of this complex pathway depends on a great number of proteins, some common for the majority of the processes and others specific for a particular autophagic event. Nevertheless, the kind of interaction between the players contributes to determining the specificity of the regulation. In a recent study, we found a new regulatory protein of starva- tion-activated autophagy called FKBP8. The absence of this protein impairs autophagy activation produced by serum starvation and its overexpression can activate the pathway in cells incubated in full media. Besides, we found that the FKBP8 function is mediated by the interaction with the PIK3C3/VPS34- containing complex. Previously, FKBP8 has been shown to participate in mito- phagy. In the latter process, FKBP8 works inducing mitochondrial fission, and also it functions as a receptor protein through its LIR domain to direct autop- hagy. In contrast to mitophagy, in starvation-activated autophagy, not the LIR but the transmembrane domain of FKBP8 is necessary for the regulatory func- tion and interaction with the PIK3C3 complex. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-07 |
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/11336/204333 Aguilera, Milton Osmar; Colombo, Maria Isabel; FKBP8, a new member of the PIK3C3/VPS34 complex; Taylor & Francis; Autophagy Reports; 8; 7-2022; 291-294 2769-4127 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/204333 |
identifier_str_mv |
Aguilera, Milton Osmar; Colombo, Maria Isabel; FKBP8, a new member of the PIK3C3/VPS34 complex; Taylor & Francis; Autophagy Reports; 8; 7-2022; 291-294 2769-4127 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/full/10.1080/27694127.2022.2100041 info:eu-repo/semantics/altIdentifier/doi/10.1080/27694127.2022.2100041 |
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 |
dc.publisher.none.fl_str_mv |
Taylor & Francis |
publisher.none.fl_str_mv |
Taylor & Francis |
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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1844614474616537088 |
score |
13.070432 |