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Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Wang, Juan ; Menon, Shekar ; Yamasaki, Akinori ; Chou, Hui-Ting ; Walz, Thomas ; Jiang, Yu ; Ferro-Novick, Susan

Proceedings of the National Academy of Sciences - PNAS, 2013-06, Vol.110 (24), p.9800-9805 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
Ypt1 recruits the Atg1 kinase to the preautophagosomal structure
Autor: Wang, Juan ; Menon, Shekar ; Yamasaki, Akinori ; Chou, Hui-Ting ; Walz, Thomas ; Jiang, Yu ; Ferro-Novick, Susan
Assuntos: Animals ; Antibodies ; Autophagy ; Autophagy-Related Protein-1 Homolog ; Autophagy-Related Proteins ; Binding sites ; Biological Sciences ; Biological transport ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cercopithecus aethiops ; COS Cells ; Gels ; Golgi Apparatus - metabolism ; Goods and services tax ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; Guanine Nucleotide Exchange Factors - genetics ; Guanine Nucleotide Exchange Factors - metabolism ; HeLa Cells ; Humans ; Immunoblotting ; Intracellular Signaling Peptides and Proteins - genetics ; Intracellular Signaling Peptides and Proteins - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Mice ; Microscopy, Fluorescence ; NIH 3T3 Cells ; Nitrogen ; Phagosomes - metabolism ; Physiological regulation ; Protein Binding ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; rab GTP-Binding Proteins - genetics ; rab GTP-Binding Proteins - metabolism ; rab1 GTP-Binding Proteins - genetics ; rab1 GTP-Binding Proteins - metabolism ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Spheroplasts ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism ; Yeasts
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2013-06, Vol.110 (24), p.9800-9805
Notas: http://dx.doi.org/10.1073/pnas.1302337110
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SourceType-Scholarly Journals-1
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Edited by Randy Schekman, University of California, Berkeley, CA, and approved April 26, 2013 (received for review February 5, 2013)
1Present address: Laboratory of Molecular Traffic, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma 371-8512, Japan.
Author contributions: J.W., T.W., Y.J., and S.F.-N. designed research; J.W., S.M., A.Y., H.-T.C., and Y.J. performed research; J.W., S.M., A.Y., H.-T.C., T.W., Y.J., and S.F.-N. analyzed data; and J.W., T.W., Y.J., and S.F.-N. wrote the paper.
Descrição: When macroautophagy, a catabolic process that rids the cells of unwanted proteins, is initiated, 30–60 nm Atg9 vesicles move from the Golgi to the preautophagosomal structure (PAS) to initiate autophagosome formation. The Rab GTPase Ypt1 and its mammalian homolog Rab1 regulate macroautophagy and two other trafficking events: endoplasmic reticulum-Golgi and intra-Golgi traffic. How a Rab, which localizes to three distinct cellular locations, achieves specificity is unknown. Here we show that transport protein particle III (TRAPPIII), a conserved autophagy-specific guanine nucleotide exchange factor for Ypt1/Rab1, is recruited to the PAS by Atg17. We also show that activated Ypt1 recruits the putative membrane curvature sensor Atg1 to the PAS, bringing it into proximity to its binding partner Atg17. Since Atg17 resides at the PAS, these events ensure that Atg1 will specifically localize to the PAS and not to the other compartments where Ypt1 resides. We propose that Ypt1 regulates Atg9 vesicle tethering by modulating the delivery of Atg1 to the PAS. These events appear to be conserved in higher cells.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Wang, Juan ; Menon, Shekar ; Yamasaki, Akinori ; Chou, Hui-Ting ; Walz, Thomas ; Jiang, Yu ; Ferro-Novick, Susan

United States: National Academy of Sciences

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