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    ATG9 autophagy protein ATG9 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851406, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The Atg1 complex, Atg9, and Vac8 recruit PI3K complex I to the pre-autophagosomal structure.

    The Atg1 complex, Atg9, and Vac8 recruit PI3K complex I to the pre-autophagosomal structure.
    Hitomi K, Kotani T, Noda NN, Kimura Y, Nakatogawa H., Free PMC Article

    07/14/2023
    The dynamin Vps1 mediates Atg9 transport to the sites of autophagosome formation.

    The dynamin Vps1 mediates Atg9 transport to the sites of autophagosome formation.
    Arlt H, Raman B, Filali-Mouncef Y, Hu Y, Leytens A, Hardenberg R, Guimarães R, Kriegenburg F, Mari M, Smaczynska-de Rooij II, Ayscough KR, Dengjel J, Ungermann C, Reggiori F., Free PMC Article

    06/2/2023
    Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway.

    Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway.
    Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S., Free PMC Article

    05/14/2022
    Atg9-centered multi-omics integration reveals new autophagy regulators in Saccharomyces cerevisiae.

    Atg9-centered multi-omics integration reveals new autophagy regulators in Saccharomyces cerevisiae.
    Peng D, Ruan C, Fu S, He C, Song J, Li H, Tu Y, Tang D, Yao L, Lin S, Shi Y, Zhang W, Zhou H, Zhu L, Ma C, Chang C, Ma J, Xie Z, Wang C, Xue Y., Free PMC Article

    04/16/2022
    Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion.

    Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion.
    Matoba K, Kotani T, Tsutsumi A, Tsuji T, Mori T, Noshiro D, Sugita Y, Nomura N, Iwata S, Ohsumi Y, Fujimoto T, Nakatogawa H, Kikkawa M, Noda NN.

    02/13/2021
    Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation.

    Reconstitution of autophagosome nucleation defines Atg9 vesicles as seeds for membrane formation.
    Sawa-Makarska J, Baumann V, Coudevylle N, von Bülow S, Nogellova V, Abert C, Schuschnig M, Graef M, Hummer G, Martens S., Free PMC Article

    12/12/2020
    Autophagy regulator Atg9 is degraded by the proteasome.

    Autophagy regulator Atg9 is degraded by the proteasome.
    Hu G, Rios L, Yan Z, Jasper AM, Luera D, Luo S, Rao H., Free PMC Article

    08/22/2020
    Atg9 vesicle trafficking is perturbed in exocyst complex temperature-sensitive mutants.

    Exocyst Subcomplex Functions in Autophagosome Biogenesis by Regulating Atg9 Trafficking.
    Singh S, Kumari R, Chinchwadkar S, Aher A, Matheshwaran S, Manjithaya R., Free PMC Article

    06/20/2020
    Data show that activated autophagy protein ATG11 (Atg11) dimerizes and tethers autophagy protein ATG9 (Atg9) vesicles.

    Atg11 tethers Atg9 vesicles to initiate selective autophagy.
    Matscheko N, Mayrhofer P, Rao Y, Beier V, Wollert T., Free PMC Article

    01/25/2020
    Septins also colocalized with autophagosomes, where they physically interacted with the autophagy proteins Atg8 and Atg9. When autophagosome degradation was blocked in septin-mutant cells, fewer autophagic structures accumulated, and an autophagy mutant defective in early stages of autophagosome biogenesis (atg1Delta), displayed decreased septin localization to the pre-autophagosomal structure.

    Septins are involved at the early stages of macroautophagy in S. cerevisiae.
    Barve G, Sridhar S, Aher A, Sahani MH, Chinchwadkar S, Singh S, K N L, McMurray MA, Manjithaya R., Free PMC Article

    09/7/2019
    Assembly of the Atg9-Atg2-Atg18 complex is important to establish phagophore-endoplasmic reticulum (ER) contact sites.

    Atg9 establishes Atg2-dependent contact sites between the endoplasmic reticulum and phagophores.
    Gómez-Sánchez R, Rose J, Guimarães R, Mari M, Papinski D, Rieter E, Geerts WJ, Hardenberg R, Kraft C, Ungermann C, Reggiori F., Free PMC Article

    07/20/2019
    Our data suggest that Sed5 plays a novel role in autophagy, by regulating the formation of Atg9-containing vesicles in the Golgi apparatus, and the genetic interaction between Sft1/2 and Sed5 is essential for autophagy.

    The Roles of the SNARE Protein Sed5 in Autophagy in Saccharomyces cerevisiae.
    Zou S, Sun D, Liang Y., Free PMC Article

    06/2/2018
    Atg9, Stp4, and Gvp36 are putative new regulators of sphingolipid homeostasis in Saccharomyces cerevisiae.

    Combining Deep Sequencing, Proteomics, Phosphoproteomics, and Functional Screens To Discover Novel Regulators of Sphingolipid Homeostasis.
    Lebesgue N, Megyeri M, Cristobal A, Scholten A, Chuartzman SG, Voichek Y, Scheltema RA, Mohammed S, Futerman AH, Schuldiner M, Heck AJ, Lemeer S.

    10/21/2017
    Finally, three sequential steps of this pathway are delineated: Atg9-dependent exit from the ER en route to autophagy, Ypt1- and core Atgs-mediated pre-autophagsomal-structure organization, and Ypt51-mediated delivery of APs to the vacuole

    A Role for Macro-ER-Phagy in ER Quality Control.
    Lipatova Z, Segev N., Free PMC Article

    04/16/2016
    This study identified Pho23 as a master transcriptional repressor for autophagy that regulates the frequency of autophagosome formation through its negative regulation of ATG9.

    Transcriptional regulation by Pho23 modulates the frequency of autophagosome formation.
    Jin M, He D, Backues SK, Freeberg MA, Liu X, Kim JK, Klionsky DJ., Free PMC Article

    02/27/2016
    PAS localization of Atg9 was normal in atg27(DeltaYSAV) cells.

    Atg27 tyrosine sorting motif is important for its trafficking and Atg9 localization.
    Segarra VA, Boettner DR, Lemmon SK., Free PMC Article

    12/19/2015
    ATG9 trafficking to phagophore assembly site depends on ATG23 and ATG27 stochiometry.

    Atg23 and Atg27 act at the early stages of Atg9 trafficking in S. cerevisiae.
    Backues SK, Orban DP, Bernard A, Singh K, Cao Y, Klionsky DJ., Free PMC Article

    09/26/2015
    TRAPPIII(trs85) is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy.

    TRAPPIII is responsible for vesicular transport from early endosomes to Golgi, facilitating Atg9 cycling in autophagy.
    Shirahama-Noda K, Kira S, Yoshimori T, Noda T.

    06/7/2014
    The Atg2-Atg18 complex and Atg9 localized to the edge of the IM, appearing as two or three dots, in close proximity to the endoplasmic reticulum exit sites.

    Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae.
    Suzuki K, Akioka M, Kondo-Kakuta C, Yamamoto H, Ohsumi Y.

    11/16/2013
    Trs85 and Ypt1 are localized to the preautophagosomal structure in an Atg9-dependent manner.

    Atg9 vesicles recruit vesicle-tethering proteins Trs85 and Ypt1 to the autophagosome formation site.
    Kakuta S, Yamamoto H, Negishi L, Kondo-Kakuta C, Hayashi N, Ohsumi Y., Free PMC Article

    03/30/2013
    Data show the PtdIns 4-kinase Pik1 is involved in Atg9 trafficking through the Golgi and is involved in both nonselective and selective types of autophagy, whereas the PtdIns4P 5-kinase Mss4 is involved in mitophagy but not nonselective autophagy.

    Phosphatidylinositol 4-kinases are required for autophagic membrane trafficking.
    Wang K, Yang Z, Liu X, Mao K, Nair U, Klionsky DJ., Free PMC Article

    01/26/2013
    It was shown that that the vast majority of Atg9 existed on cytoplasmic mobile vesicles that were derived from the Golgi apparatus in a process involving Atg23 and Atg27. Only a few Atg9 vesicles were needed for a single round of forming autophagosomes.

    Atg9 vesicles are an important membrane source during early steps of autophagosome formation.
    Yamamoto H, Kakuta S, Watanabe TM, Kitamura A, Sekito T, Kondo-Kakuta C, Ichikawa R, Kinjo M, Ohsumi Y., Free PMC Article

    10/20/2012
    Data show that membrane that contains Atg9 is delivered to the autophagosome from the Golgi-endosomal system rather than from the ER or mitochondria.

    Membrane delivery to the yeast autophagosome from the Golgi-endosomal system.
    Ohashi Y, Munro S., Free PMC Article

    03/19/2011
    The role of Atg9 trafficking in yeast and mammalian autophagy, is summarised.

    New insights into the function of Atg9.
    Webber JL, Tooze SA.

    04/12/2010
    in autophagy-inducing condition, Atg9 is recruited to the pre-autophagosomal structure in a manner dependent on Atg17

    Atg17 recruits Atg9 to organize the pre-autophagosomal structure.
    Sekito T, Kawamata T, Ichikawa R, Suzuki K, Ohsumi Y.

    03/22/2010
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