MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins. (Articolo in rivista)

Type
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  • MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins. (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.4161/auto.21857 (literal)
Alternative label
  • David Colecchia, Angela Strambi, Sveva Sanzone, Carlo Iavarone, Matteo Rossi, Claudia Dall'Armi, Federica Piccioni, Arturo Verrotti di Pianella and Mario Chiariello (2012)
    MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins.
    in Autophagy
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • David Colecchia, Angela Strambi, Sveva Sanzone, Carlo Iavarone, Matteo Rossi, Claudia Dall'Armi, Federica Piccioni, Arturo Verrotti di Pianella and Mario Chiariello (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.landesbioscience.com/journals/autophagy/article/21857/?nocache=420974560# (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 8 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 12 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • David Colecchia: Istituto Toscano Tumori-Core Research Laboratory; Signal Transduction Unit; AOU Senese; Siena, Italy; Università degli Studi di Siena; Siena, Italy Angela Strambi: Istituto Toscano Tumori-Core Research Laboratory; Signal Transduction Unit; AOU Senese; Siena, Italy; Istituto di Fisiologia Clinica; Sede di Siena; CNR; Siena, Italy Sveva Sanzone: Istituto Toscano Tumori-Core Research Laboratory; Signal Transduction Unit; AOU Senese; Siena, Italy Carlo Iavarone: Istituto di Endocrinologia e Oncologia Sperimentale; CNR; Napoli, Italy; Immunology US, Novartis Vaccines and Diagnostics; Cambridge, MA USA Matteo Rossi: Istituto Toscano Tumori-Core Research Laboratory; Signal Transduction Unit; AOU Senese; Siena, Italy; Università degli Studi di Siena; Siena, Italy Claudia Dall'Armi: Department of Pathology and Cell Biology & Taub Institute for Research on Alzheimer's Disease and the Aging Brain; Columbia University Medical Center; New York, NY USA Federica Piccioni: CEINGE-Biotecnologie Avanzate & Dipartimento di Biochimica e Biotecnologie Mediche; Università degli Studi di Napoli; Napoli, Italy Arturo Verrotti di Pianella: CEINGE-Biotecnologie Avanzate & Dipartimento di Biochimica e Biotecnologie Mediche; Università degli Studi di Napoli; Napoli, Italy Mario Chiariello: Istituto di Fisiologia Clinica; Sede di Siena; CNR; Siena, Italy; Istituto Toscano Tumori-Core Research Laboratory; Signal Transduction Unit; AOU Senese; Siena, Italy (literal)
Titolo
  • MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP proteins. (literal)
Abstract
  • Macroautophagy (hereafter referred to as autophagy) is an evolutionarily conserved catabolic process necessary for normal recycling of cellular constituents and for appropriate response to cellular stress. Although several genes belonging to the core molecular machinery involved in autophagosome formation have been discovered, relatively little is known about the nature of signaling networks controlling autophagy upon intracellular or extracellular stimuli. We discovered ATG8-like proteins (MAP1LC3B, GABARAP and GABARAPL1) as novel interactors of MAPK15/ERK8, a MAP kinase involved in cell proliferation and transformation. Based on the role of these proteins in the autophagic process, we demonstrated that MAPK15 is indeed localized to autophagic compartments and increased, in a kinase-dependent fashion, ATG8-like proteins lipidation, autophagosome formation and SQSTM1 degradation, while decreasing LC3B inhibitory phosphorylation. Interestingly, we also identified a conserved LC3-interacting region (LIR) in MAPK15 responsible for its interaction with ATG8-like proteins, for its localization to autophagic structures and, consequently, for stimulation of the formation of these compartments. Furthermore, we reveal that MAPK15 activity was induced in response to serum and amino-acid starvation and that this stimulus, in turn, required endogenous MAPK15 expression to induce the autophagic process. Altogether, these results suggested a new function for MAPK15 as a regulator of autophagy, acting through interaction with ATG8 family proteins. Also, based on the key role of this process in several human diseases, these results supported the use of this MAP kinase as a potential novel therapeutic target. (literal)
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