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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/204333

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spelling 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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