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dc.contributor.author
Fader Kaiser, Claudio Marcelo

dc.contributor.author
Aguilera, Milton Osmar

dc.contributor.author
Colombo, Maria Isabel

dc.date.available
2018-01-02T18:44:38Z
dc.date.issued
2014-09
dc.identifier.citation
Colombo, Maria Isabel; Aguilera, Milton Osmar; Fader Kaiser, Claudio Marcelo; Autophagy response: manipulating the mTOR-controlled machinery by amino acids and pathogens; Springer Wien; Amino Acids; 47; 10; 9-2014; 2101-2112
dc.identifier.issn
0939-4451
dc.identifier.uri
http://hdl.handle.net/11336/32010
dc.description.abstract
Macroautophagy is a self-degradative process that normally maintains cellular homeostasis via a lysosomal pathway. It is induced by different stress signals, including nutrients and growth factors’ restriction as well as pathogen invasions. These stimuli are modulated by the serine/threonine protein kinase mammalian target of rapamycin (mTOR) which control not only autophagy but also protein translation and gene expression. This review focuses on the important role of mTOR as a master regulator of cell growth and the autophagy pathway. Here, we have discussed the role of intracellular amino acid availability and intracellular pH in the redistribution of autophagic structures, which may contribute to mammalian target of rapamycin complex 1 (mTORC1) activity regulation. We have also discussed that mTORC1 complex and components of the autophagy machinery are localized at the lysosomal surface, representing a fascinating mechanism to control the metabolism, cellular clearance and also to restrain invading intracellular pathogens.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer Wien

dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Autophagy
dc.subject
Mtor
dc.subject
Amino Acids
dc.subject
Pathogens
dc.subject
Lc3
dc.subject.classification
Otras Ciencias Biológicas

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Ciencias Biológicas

dc.subject.classification
CIENCIAS NATURALES Y EXACTAS

dc.title
Autophagy response: manipulating the mTOR-controlled machinery by amino acids and pathogens
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-12-29T14:12:13Z
dc.identifier.eissn
1438-2199
dc.journal.volume
47
dc.journal.number
10
dc.journal.pagination
2101-2112
dc.journal.pais
Austria

dc.journal.ciudad
Viena
dc.description.fil
Fil: Fader Kaiser, Claudio Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
dc.description.fil
Fil: Aguilera, Milton Osmar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
dc.description.fil
Fil: Colombo, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
dc.journal.title
Amino Acids

dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs00726-014-1835-7
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00726-014-1835-7
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