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Autophagic Nutrient Recycling in Arabidopsis Directed by the ATG8 and ATG12 Conjugation Pathways

Thompson, Allison R., Doelling, Jed H., Suttangkakul, Anongpat, Vierstra, Richard D.·2005·Plant Physiology
DOI 10.1104/pp.105.060673
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Abstract

Autophagy is an important mechanism for nonselective intracellular breakdown whereby cytosol and organelles are encapsulated in vesicles, which are then engulfed and digested by lytic vacuoles/lysosomes. In yeast, this encapsulation employs a set of autophagy (ATG) proteins that direct the conjugation of two ubiquitin-like protein tags, ATG8 and ATG12, to phosphatidylethanolamine and the ATG5 protein, respectively. Using an Arabidopsis (Arabidopsis thaliana) atg7 mutant unable to ligate either tag, we previously showed that the ATG8/12 conjugation system is important for survival under nitrogen-limiting growth conditions. By reverse-genetic analyses of the single Arabidopsis gene encoding ATG5, we show here that the subpathway that forms the ATG12-ATG5 conjugate also has an essential role in plant nutrient recycling. Similar to plants missing ATG7, those missing ATG5 display early senescence and are hypersensitive to either nitrogen or carbon starvation, which is accompanied by a more rapid loss of organellar and cytoplasmic proteins. Multiple ATG8 isoforms could be detected immunologically in seedling extracts. Their abundance was substantially elevated in both the atg5 and atg7 mutants, caused in part by an increase in abundance of several ATG8 mRNAs. Using a green fluorescent protein-ATG8a fusion in combination with concanamycin A, we also detected the accumulation of autophagic bodies inside the vacuole. This accumulation was substantially enhanced by starvation but blocked in the atg7 background. The use of this fusion in conjunction with atg mutants now provides an important marker to track autophagic vesicles in planta.

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Citations

Cites

  • Molecular dissection of autophagy: two ubiquitin-like systems

    Ohsumi, Y. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056522 · Cited by 1,240 · cited 4×

    “Here, individual proteins, protein complexes, and entire organelles become engulfed in membrane-bound vesicles, which are delivered to the vacuole (yeast/plants) or lysosome (animals; Ohsumi, 2001; Klionsky, 2004; Thompson and Vierstra, 2005).”
    BackgroundInfluential

  • Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast

    Kirisako, T., Baba, M., Ishihara, N., Miyazawa, K., Ohsumi, M., Yoshimori, T., Noda, T., & Ohsumi, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.435 · Cited by 881 · cited 1×

    “The inclusion of urea was based on previous studies with yeast ATG8 showing that the PE-conjugate migrates faster than free ATG8 under this electrophoretic condition (Kirisako et al., 1999).”
    Method

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Metadata

Authors
Thompson, A. R., Doelling, J. H., Suttangkakul, A., & Vierstra, R. D.
Affiliations
Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706
Venue
Plant Physiology
Publisher
Oxford University Press (OUP)
Published
2005-07-22
Volume
138
Issue
4
Pages
2097-2110
ISSN
  • 1532-2548
  • 0032-0889
DOI
10.1104/pp.105.060673
Cited by
574
References
2
Language
en
Licence
academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)

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