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    ATG8 ubiquitin-like protein ATG8 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852200, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Effect of ATG8 or SAC1 deficiency on the cell proliferation and lifespan of the long-lived PMT1 deficiency yeast cells.

    Effect of ATG8 or SAC1 deficiency on the cell proliferation and lifespan of the long-lived PMT1 deficiency yeast cells.
    Cui H, Cui X, Yang X, Cui X, Sun Y, Yuan D, Cui Q, Deng Y, Sun E, Chen YQ, Guo H, Deng Z, Wang J, Xu S, Sun X, Wei Z, Liu X.

    02/20/2024
    Biophysical characterization of the interaction of Atg8 with a disordered region of Nup159 involved in selective autophagy of the nuclear pore complex.

    Biophysical characterization of the interaction of Atg8 with a disordered region of Nup159 involved in selective autophagy of the nuclear pore complex.
    Kim R, Koh J.

    04/16/2022
    Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.

    Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.
    Barz S, Kriegenburg F, Sánchez-Martín P, Kraft C., Free PMC Article

    12/4/2021
    Membrane perturbation by lipidated Atg8 underlies autophagosome biogenesis.

    Membrane perturbation by lipidated Atg8 underlies autophagosome biogenesis.
    Maruyama T, Alam JM, Fukuda T, Kageyama S, Kirisako H, Ishii Y, Shimada I, Ohsumi Y, Komatsu M, Kanki T, Nakatogawa H, Noda NN.

    09/25/2021
    TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes.

    TORC1 inactivation stimulates autophagy of nucleoporin and nuclear pore complexes.
    Tomioka Y, Kotani T, Kirisako H, Oikawa Y, Kimura Y, Hirano H, Ohsumi Y, Nakatogawa H., Free PMC Article

    03/20/2021
    Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.

    Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement.
    Wang S, Li Y, Ma C., Free PMC Article

    02/27/2021
    Role of Atg8 in the regulation of vacuolar membrane invagination.

    Role of Atg8 in the regulation of vacuolar membrane invagination.
    Ishii A, Kurokawa K, Hotta M, Yoshizaki S, Kurita M, Koyama A, Nakano A, Kimura Y., Free PMC Article

    11/21/2020
    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
    The authors find that Mon1-Ccz1 directly binds to Atg8, the yeast homolog of the members of the mammalian LC3 protein family.

    Molecular mechanism to target the endosomal Mon1-Ccz1 GEF complex to the pre-autophagosomal structure.
    Gao J, Langemeyer L, Kümmel D, Reggiori F, Ungermann C., Free PMC Article

    08/3/2019
    The purified autophagy receptor ATG19 is recruited to affinity resins via a suitable tag and then added to fluorescently labeled ATG8 in solution. The relative strength of the interaction is assessed by determination of the fluorescence intensity on the surface of the bead at an equilibrium binding state. The relative binding strength is determined.

    Studies of Receptor-Atg8 Interactions During Selective Autophagy.
    Abert C, Martens S.

    06/29/2019
    Msn2 and Msn4 promote ATG8 expression downstream of the histone deacetylase complex (HDAC) subunit Ume6, a previously identified negative regulator of ATG8 expression.

    Stress-response transcription factors Msn2 and Msn4 couple TORC2-Ypk1 signaling and mitochondrial respiration to ATG8 gene expression and autophagy.
    Vlahakis A, Lopez Muniozguren N, Powers T., Free PMC Article

    06/8/2019
    Atg7 recognizes Atg8 through multiple steps, which would be necessary to induce a conformational change in Atg7 that is optimal for the activation reaction.

    Atg7 Activates an Autophagy-Essential Ubiquitin-like Protein Atg8 through Multi-Step Recognition.
    Yamaguchi M, Satoo K, Suzuki H, Fujioka Y, Ohsumi Y, Inagaki F, Noda NN.

    03/23/2019
    ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8

    ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8.
    Skytte Rasmussen M, Mouilleron S, Kumar Shrestha B, Wirth M, Lee R, Bowitz Larsen K, Abudu Princely Y, O'Reilly N, Sjøttem E, Tooze SA, Lamark T, Johansen T., Free PMC Article

    03/31/2018
    findings show Atg4 is recruited onto autophagosomal membranes by direct binding to Atg8 via two evolutionarily conserved Atg8 recognition sites; propose a model where Atg4 activity on autophagosomal membranes depends on cooperative action of at least 2 sites within Atg4, in which one functions as a constitutive Atg8 binding module, while the other has a preference toward phosphatidylethanolamine-bound Atg8

    Conserved Atg8 recognition sites mediate Atg4 association with autophagosomal membranes and Atg8 deconjugation.
    Abreu S, Kriegenburg F, Gómez-Sánchez R, Mari M, Sánchez-Wandelmer J, Skytte Rasmussen M, Soares Guimarães R, Zens B, Schuschnig M, Hardenberg R, Peter M, Johansen T, Kraft C, Martens S, Reggiori F., Free PMC Article

    01/27/2018
    Mechanism of cargo-directed Atg8 conjugation during selective autophagy has been described.

    Mechanism of cargo-directed Atg8 conjugation during selective autophagy.
    Fracchiolla D, Sawa-Makarska J, Zens B, Ruiter A, Zaffagnini G, Brezovich A, Romanov J, Runggatscher K, Kraft C, Zagrovic B, Martens S., Free PMC Article

    11/25/2017
    Results provide evidence that delipidation of Atg8-PE is important for efficient isolation membranes expansion in Saccharomyces cerevisiae.

    Atg4 plays an important role in efficient expansion of autophagic isolation membranes by cleaving lipidated Atg8 in Saccharomyces cerevisiae.
    Hirata E, Ohya Y, Suzuki K., Free PMC Article

    09/30/2017
    Deletion of ATG8 causes a decrease in lipid droplets (LD) quantity in cells at stationary phase.

    Autophagy-independent function of Atg8 in lipid droplet dynamics in yeast.
    Maeda Y, Oku M, Sakai Y.

    06/3/2017
    one Atg19 molecule has the ability to interact with multiple Atg8 proteins simultaneously, resulting in a high-avidity interaction that may confer specific binding to the Atg8-coated autophagosomal membrane on which Atg8 is concentrated.

    Accessory Interaction Motifs in the Atg19 Cargo Receptor Enable Strong Binding to the Clustered Ubiquitin-related Atg8 Protein.
    Abert C, Kontaxis G, Martens S., Free PMC Article

    05/20/2017
    Amelioration of Atg32 expression and attenuation of Atg8-phosphatidylmonomethylethanolamine conjugation markedly rescue mitophagy in opi null cells.

    Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recycling.
    Sakakibara K, Eiyama A, Suzuki SW, Sakoh-Nakatogawa M, Okumura N, Tani M, Hashimoto A, Nagumo S, Kondo-Okamoto N, Kondo-Kakuta C, Asai E, Kirisako H, Nakatogawa H, Kuge O, Takao T, Ohsumi Y, Okamoto K., Free PMC Article

    02/27/2016
    Here we describe assays for the in vitro reconstitution of the Atg8 lipidation reaction using recombinantly expressed and purified proteins derived from Saccharomycescerevisiae in combination with small and giant unilamellar vesicles.

    In vitro systems for Atg8 lipidation.
    Zens B, Sawa-Makarska J, Martens S., Free PMC Article

    11/28/2015
    Atg21 thus defines PI3P-dependently the lipidation site by linking and organising the E3 ligase complex and Atg8 at the PAS.

    PI3P binding by Atg21 organises Atg8 lipidation.
    Juris L, Montino M, Rube P, Schlotterhose P, Thumm M, Krick R., Free PMC Article

    06/20/2015
    Study identified ubiquitin-Atg8 adaptors termed CUET proteins, comprising the ubiquitin-binding CUE-domain protein Cue5 from yeast and its human homolog Tollip. Cue5 collaborates with Rsp5 ubiquitin ligase, and the corresponding yeast mutants accumulate aggregation-prone proteins and are vulnerable to polyQ protein expression.

    Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family.
    Lu K, Psakhye I, Jentsch S.

    02/7/2015
    Cargo binding to Atg19 unmasks additional Atg8 binding sites to mediate membrane-cargo apposition during selective autophagy.

    Cargo binding to Atg19 unmasks additional Atg8 binding sites to mediate membrane-cargo apposition during selective autophagy.
    Sawa-Makarska J, Abert C, Romanov J, Zens B, Ibiricu I, Martens S., Free PMC Article

    08/9/2014
    Atg1, Atg8 and the Atg16-Atg12-Atg5 complex were present at both the VICS and the cup-shaped IM.

    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
    Selective autophagy receptors interact with two proteins of the core autophagic machinery: the scaffold protein Atg11 and the ubiquitin-like protein Atg8.

    Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11.
    Farré JC, Burkenroad A, Burnett SF, Subramani S., Free PMC Article

    10/26/2013
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