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  Molecular Mechanism of Autophagic Membrane-Scaffold Assembly and Disassembly

Kaufmann, A., Beier, V., Franquelim, H. G., & Wollert, T. (2014). Molecular Mechanism of Autophagic Membrane-Scaffold Assembly and Disassembly. CELL, 156(3), 469-481. doi:10.1016/j.cell.2013.12.022.

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 Urheber:
Kaufmann, Anna1, Autor           
Beier, Viola1, Autor           
Franquelim, Henri G.2, Autor           
Wollert, Thomas1, Autor           
Affiliations:
1Wollert, Thomas / Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565175              
2Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Schlagwörter: VACUOLE TARGETING PATHWAY; FAMILY INTERACTING MOTIF; ATG12-ATG5 CONJUGATE; PROTEIN LIPIDATION; YEAST AUTOPHAGY; ATG8; CYTOPLASM; COMPLEX; BINDING; MACROAUTOPHAGY
 Zusammenfassung: Autophagy is a catabolic pathway that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. A key step in the pathway is the covalent conjugation of the ubiquitin-related protein Atg8 to phosphatidylethanolamine (Atg8-PE) in autophagic membranes by a complex consisting of Atg16 and the Atg12Atg5 conjugate. Atg8 controls the expansion of autophagic precursor membranes, but the underlying mechanism remains unclear. Here, we reconstitute Atg8 conjugation on giant unilamellar vesicles and supported lipid bilayers. We found that Atg8-PE associates with Atg12-Atg5-Atg16 into a membrane scaffold. By contrast, scaffold formation is counteracted by the mitochondrial cargo adaptor Atg32 through competition with Atg12-Atg5 for Atg8 binding. Atg4, previously known to recycle Atg8 from membranes, disassembles the scaffold. Importantly, mutants of Atg12 and Atg16 deficient in scaffold formation in vitro impair autophagy in vivo. This suggests that autophagic scaffolds are critical for phagophore biogenesis and thus autophagy.

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Sprache(n): eng - English
 Datum: 2014
 Publikationsstatus: Erschienen
 Seiten: 13
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000330580800014
DOI: 10.1016/j.cell.2013.12.022
 Art des Abschluß: -

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Titel: CELL
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Seiten: - Band / Heft: 156 (3) Artikelnummer: - Start- / Endseite: 469 - 481 Identifikator: ISSN: 0092-8674