Biology and trafficking of ATG9 and ATG16L1, two proteins that regulate autophagosome formation

被引:66
|
作者
Zavodszky, Eszter [1 ]
Vicinanza, Mariella [1 ]
Rubinsztein, David C. [1 ]
机构
[1] Univ Cambridge, Addenbrookes Hosp, Dept Med Genet, Cambridge Inst Med Res, Cambridge CB2 0XY, England
基金
英国惠康基金;
关键词
Autophagy; Atg9; Atg16; Phagophore; Membrane trafficking; GENOME-WIDE ASSOCIATION; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; LC3; LIPIDATION; CONJUGATION SYSTEM; ISOLATION MEMBRANE; CROHN-DISEASE; COMPLEX; YEAST; GOLGI;
D O I
10.1016/j.febslet.2013.04.025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Autophagy is a highly conserved intracytoplasmic degradation pathway for proteins, oligomers, organelles and pathogens. It initiates with the formation of a cup-shaped double membrane structure called the phagophore. The membrane origin for autophagosomes has been a key question for the field. ATG9 and ATG16L1, or their yeast orthologues, are key proteins that regulate autophagosome biogenesis, and may be associated with distinct membrane sources. Here we review the biology of autophagy with a focus on ATG16L1 and ATG9, and we summarise the current knowledge of their trafficking in relation to autophagic stimuli and autophagosome formation. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1988 / 1996
页数:9
相关论文
共 50 条
  • [31] RHOD mediates ATG9A trafficking to promote autophagosome formation during autophagy in cancer
    Wang, Sijia
    Ren, Jing
    Chi, Jinghan
    Guan, Yifei
    Zheng, Ran
    Wang, Juan
    Liu, Xinhui
    Huang, Hua
    AUTOPHAGY, 2025,
  • [32] Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi membranes during autophagy
    Takahashi, Yoshinori
    Meyerkord, Cheryl L.
    Hori, Tsukasa
    Runkle, Kristin
    Fox, Todd E.
    Kester, Mark
    Loughran, Thomas P.
    Wang, Hong-Gang
    AUTOPHAGY, 2011, 7 (01) : 61 - 73
  • [33] Polymorphisms in the ATG16L1 Gene are Associated with Psoriasis Vulgaris
    Douroudis, Konstantinos
    Kingo, Kuelli
    Traks, Tanel
    Reimann, Ene
    Raud, Kristi
    Raetsep, Ranno
    Moessner, Rotraut
    Silm, Helgi
    Vasar, Eero
    Koks, Sulev
    ACTA DERMATO-VENEREOLOGICA, 2012, 92 (01) : 85 - 87
  • [34] Structure of the WIPI3/ATG16L1 Complex Reveals the Molecular Basis for the Recruitment of the ATG12∼ATG5-ATG16L1 Complex by WIPI3
    Gong, Xinyu
    Wang, Yingli
    Zhou, Yuqian
    Pan, Lifeng
    CELLS, 2024, 13 (24)
  • [35] FIP200 regulates targeting of Atg16L1 to the isolation membrane
    Nishimura, Taki
    Kaizuka, Takeshi
    Cadwell, Ken
    Sahani, Mayurbhai H.
    Saitoh, Tatsuya
    Akira, Shizuo
    Virgin, Herbert W.
    Mizushima, Noboru
    EMBO REPORTS, 2013, 14 (03) : 284 - 291
  • [36] The Crohn's disease: associated ATG16L1 variant and Salmonella invasion
    Messer, Jeannette S.
    Murphy, Stephen F.
    Logsdon, Mark F.
    Lodolce, James P.
    Grimm, Wesley A.
    Bartulis, Sarah J.
    Vogel, Tiphanie P.
    Burn, Melisa
    Boone, David L.
    BMJ OPEN, 2013, 3 (06):
  • [37] Intrinsic lipid binding activity of ATG16L1 supports efficient membrane anchoring and autophagy
    Dudley, Leo J.
    Cabodevilla, Ainara G.
    Makar, Agata N.
    Sztacho, Martin
    Michelberger, Tim
    Marsh, Joseph A.
    Houston, Douglas R.
    Martens, Sascha
    Jiang, Xuejun
    Gammoh, Noor
    EMBO JOURNAL, 2019, 38 (09)
  • [38] Identification, biochemical characterization and crystallization of the central region of human ATG16L1
    Archna, Archna
    Scrima, Andrea
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2017, 73 : 560 - 567
  • [39] An alteration in ATG16L1 stability in Crohn disease
    Lassen, Kara G.
    Xavier, Ramnik J.
    AUTOPHAGY, 2014, 10 (10) : 1858 - 1860
  • [40] Targeting the ATG5-ATG16L1 Protein-Protein Interaction with a Hydrocarbon-Stapled Peptide Derived from ATG16L1 for Autophagy Inhibition
    Cui, Jin
    Ogasawara, Yuta
    Kurata, Ikuko
    Matoba, Kazuaki
    Fujioka, Yuko
    Noda, Nobuo N.
    Shibasaki, Masakatsu
    Watanabe, Takumi
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2022, 144 (38) : 17671 - 17679