Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy.

Vargas, Jose Norberto S; Wang, Chunxin; Bunker, Eric; Hao, Ling; Maric, Dragan; Schiavo, Giampietro; Randow, Felix; Youle, Richard J

Vargas, Jose Norberto S; Wang, Chunxin; Bunker, Eric; Hao, Ling; Maric, Dragan; Schiavo, Giampietro; Randow, Felix; Youle, Richard J.

Afiliación

Vargas JNS; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA; Department of Neuromuscular Disorders, UCL Institute of Neurology, University College London, London WC1N 3BG, UK.
Wang C; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Bunker E; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Hao L; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Maric D; Flow and Imaging Cytometry Core Facility, National Institute of Neurological Diseases and Stroke, Bethesda, MD 20892, USA.
Schiavo G; Department of Neuromuscular Disorders, UCL Institute of Neurology, University College London, London WC1N 3BG, UK; UK Dementia Research Institute at UCL, UCL Queen Square Institute of Neurology, University College London, London WC1E 6BT, UK; Discoveries Centre for Regenerative and Precision Medicin
Randow F; MRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK; University of Cambridge, Department of Medicine, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Youle RJ; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: youler@ninds.nih.gov.

Mol Cell ; 74(2): 347-362.e6, 2019 04 18.

Article en En | MEDLINE | ID: mdl-30853401

Asunto(s)

Homólogo de la Proteína 1 Relacionada con la Autofagia/genética; Autofagia/genética; Proteínas Nucleares/genética; Proteínas Serina-Treonina Quinasas/genética; Quinasas de la Proteína-Quinasa Activada por el AMP; Proteínas Relacionadas con la Autofagia; Repeticiones Palindrómicas Cortas Agrupadas y Regularmente Espaciadas/genética; Células HeLa; Humanos; Mitocondrias/química; Mitocondrias/genética; Complejos Multiproteicos/química; Complejos Multiproteicos/genética; Peroxisomas/química; Peroxisomas/genética; Fosforilación; Proteínas Quinasas/genética; Multimerización de Proteína; Proteínas Tirosina Quinasas/química; Proteínas Tirosina Quinasas/genética; Transducción de Señal/genética; Serina-Treonina Quinasas TOR/genética

Palabras clave

ATG13; FIP200; P62; PINK1; Parkin; TAX1BP1; lysosome; mitochondria; mitophagy; optineurin

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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Autofagia / Proteínas Nucleares / Proteínas Serina-Treonina Quinasas / Homólogo de la Proteína 1 Relacionada con la Autofagia Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Mol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2019 Tipo del documento: Article País de afiliación: Reino Unido

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