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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

Show all 2 references

Research works printed but not linked: 43

  1. Brouquisse R, Gaudillere JP, Raymond P (1998) Induction of a carbon-starvation-related proteolysis in whole maize plants submitted to light/dark cycles and to extended darkness. Plant Physiol117:1281–1291 · DOI
  2. Buchanan-Wollaston V, Page T, Harrison E, Breeze E, Lim PO, Nam HG, Lin JF, Wu SH, Swidzinski J, Ishizaki K, et al (2005) Comparative transcriptome analysis reveals significant differences in gene expression and signaling pathways between developmental and dark/starvation-induced senescence in Arabidopsis. Plant J42:567–585 · DOI
  3. Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana.Plant J16:735–743 · DOI
  4. Contento AL, Kim SJ, Bassham DC (2004) Transcriptome profiling of the response of Arabidopsis suspension culture cells to Suc starvation. Plant Physiol135:2330–2347 · DOI
  5. Cutler SR, Ehrhardt DW, Griffitts JS, Somerville CR (2000) Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc Natl Acad Sci USA97:3718–3723 · DOI
  6. Doelling JH, Walker JM, Friedman EM, Thompson AR, Vierstra RD (2002) The APG8/12-activating enzyme APG7 is required for proper nutrient recycling and senescence in Arabidopsis thaliana.J Biol Chem277:33105–33114 · DOI
  7. Drose S, Bindseil KU, Bowmama EJ, Siebers A, Zeeck A, Altendorf K (1993) Inhibitory effect of modified bafilomycins and concanamycins and P- and V-type adenosinetriphosphatases. Biochemistry32:3902–3906 · DOI
  8. Giuliano G, Hoffman NE, Ko K, Scolnik PA, Cashmore AR (1988) A light-entrained circadian clock controls transcription of several plant genes. EMBO J7:3635–3642 · DOI
  9. Giulietti A, Overbergh L, Valckx D, Decallonne B, Bouillon R, Mathieu C (2001) An overview of real-time quantitative PCR: applications to quantify cytokine gene expression. Methods25:386–401 · DOI
  10. Guo R, Luo M, Weinstein JD (1998) Magnesium-chelatase from developing pea leaves: characterization of a soluble extract from chloroplasts and resolution into three required protein fractions. Plant Physiol116:605–615 · DOI
  11. Hammond EM, Brunet CL, Johnson GD, Parkhill J, Milner AE, Brady G, Gregory CD, Grand RJ (1998) Homology between a human apoptosis specific protein and the product of APG5, a gene involved in autophagy in yeast. FEBS Lett425:391–395 · DOI
  12. Hanaoka H, Noda T, Shirano Y, Kato T, Hayashi H, Shibata D, Tabata S, Ohsumi Y (2002) Leaf senescence and starvation-induced chlorosis are accelerated by the disruption of an Arabidopsis autophagy gene. Plant Physiol129:1181–1193 · DOI
  13. Hoffmann A, Nebenfuhr A (2004) Dynamic rearrangement of transvacuolar strands in BY-2 cells imply a role of myosin in remodeling the plant actin cytoskeleton. Protoplasma224:201–210 · DOI
  14. Huang WP, Klionsky DJ (2002) Autophagy in yeast: a review of the molecular machinery. Cell Struct Funct27:409–420 · DOI
  15. Kametaka S, Matsuura A, Wada Y, Ohsumi Y (1996) Structural and functional analyses of APG5, a gene involved in autophagy in yeast. Gene178:139–143 · DOI
  16. Klionsky DJ, Cregg JM, Dunn WA, Emr SD, Sakai Y, Sandoval IV, Sibirny A, Subramani S, Thumm M, Veenhuis M, et al (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell5:539–545 · DOI
  17. Luethy MH, Horak A, Elthon TE (1993) Monoclonal antibodies to the α- and β-subunits of the plant mitochondrial F1-ATPase. Plant Physiol101:931–937 · DOI
  18. Ma L, Sun N, Liu X, Jiao Y, Zhao H, Deng X-W (2005) Organ-specific expression of Arabidopsis genome during development. Plant Physiol138:80–91 · DOI
  19. Marino G, Uria JA, Puente XS, Quesada V, Bordallo J, Lopez-Otin C (2003) Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy. J Biol Chem278:3671–3678 · DOI
  20. Matsuoka K, Higuchi T, Maeshima M, Nakamura K (1997) A vacuolar-type H+-ATPase in a nonvacuolar organelle is required for the sorting of soluble vacuolar protein precursors in tobacco cells. Plant Cell9:533–546 · DOI
  21. Matt P, Schurr U, Klein D, Krapp A, Stitt M (1998) Growth of tobacco in short-day conditions leads to high starch, low sugars, altered diurnal changes in the NIA transcript and low nitrate reductase activity, and inhibition of amino acid synthesis. Planta207:27–41 · DOI
  22. Melendez A, Talloczy Z, Seaman M, Eskelinen EL, Hall DH, Levine B (2003) Autophagy genes are essential for dauer development and life-span extension in C. elegans.Science301:1387–1391 · DOI · Paper page
  23. Menand B, Desnos T, Nussaume L, Berger F, Bouchez D, Meyer C, Robaglia C (2002) Expression and disruption of the Arabidopsis TOR (target of rapamycin) gene. Proc Natl Acad Sci USA99:6422–6427 · DOI
  24. Mizushima N, Yamamoto A, Hatano M, Kobayashi Y, Kabeya Y, Suzuki K, Tokuhisa T, Ohsumi Y, Yoshimori T (2001) Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J Cell Biol152:657–668 · DOI · Paper page
  25. Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell15:1101–1111 · DOI · Paper page
  26. Moriyasu Y, Klionsky DJ (2004) Autophagy in plants. In DJ Klionsky, ed, Autophagy. Eurekah.com/Landes Bioscience, Georgetown, TX, pp 208–215 · DOI
  27. Moriyasu Y, Ohsumi Y (1996) Autophagy in tobacco suspension-cultured cells in response to sucrose starvation. Plant Physiol111:1233–1241 · DOI
  28. Niwa Y, Kato T, Tabata S, Seki M, Kobayashi M, Shinozaki K, Moriyasu Y (2004) Disposal of chloroplasts with abnormal function into the vacuole in Arabidopsis thaliana cotyledon cells. Protoplasma223:229–232 · DOI
  29. Otto GP, Wu MY, Kazgan N, Anderson OR, Kessin RH (2003) Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum.J Biol Chem278:17636–17645 · DOI · Paper page
  30. Rose TL, Bonneau L, Der C, Marty-Mazars D, Marty F (2005) Starvation-induced expression of autophagy-related genes in Arabidopsis. Biol Cell doi/10.1042/BC20040516 · DOI
  31. Sessions A, Burke E, Presting G, Aux G, McElver J, Patton D, Dietrich B, Ho P, Bacwaden J, Ko C, et al (2002) A high-throughput Arabidopsis reverse genetics system. Plant Cell14:2985–2994 · DOI
  32. Smalle J, Kurepa J, Yang P, Babiychuk E, Kushnir S, Durski A, Vierstra RD (2002) Cytokinin growth responses in Arabidopsis involve the 26S proteasome subunit RPN12. Plant Cell14:17–32 · DOI
  33. Smalle J, Vierstra RD (2004) The ubiquitin 26S proteasome proteolytic pathway. Annu Rev Plant Biol55:555–590 · DOI
  34. Surpin M, Zheng H, Morita MT, Saito C, Avila E, Blakeslee JJ, Bandyopadhyay A, Kovaleva V, Carter D, Murphy A, et al (2003) The VTI family of SNARE proteins is necessary for plant viability and mediates different protein transport pathways. Plant Cell15:2885–2899 · DOI
  35. Suzuki K, Kirisako T, Kamada Y, Mizushima N, Noda T, Ohsumi Y (2001) The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation. EMBO J20:5971–5981 · DOI
  36. Takatsuka C, Inoue Y, Matsuoka K, Moriyasu Y (2004) 3-Methyladenine inhibits autophagy in tobacco culture cells under sucrose starvation conditions. Plant Cell Physiol45:265–274 · DOI
  37. Tamura K, Shimada T, Ono E, Tanaka Y, Nagatani A, Higashi S, Watanabe M, Nishimura M, Hara-Nishimura I (2003) Why green fluorescent fusion proteins have not been observed in the vacuoles of higher plants. Plant J35:545–555 · DOI
  38. Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E (2002) Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p. J Biol Chem277:13739–13744 · DOI
  39. Thompson AR, Vierstra RD (2005) Autophagic recycling: lessons from yeast help define the process in plants. Curr Opin Plant Biol8:165–173 · DOI
  40. Thumm M, Kadowaki T (2001) The loss of Drosophila APG4/AUT2 function modifies the phenotypes of cut and Notch signaling pathway mutants. Mol Genet Genomics266:657–663 · DOI
  41. Vierstra RD (1996) Proteolysis in plants: mechanisms and functions. Plant Mol Biol32:275–302 · DOI
  42. Weaver LM, Gan S, Quirino B, Amasino RM (1998) A comparison of the expression patterns of several senescence-associated genes in response to stress and hormone treatment. Plant Mol Biol37:455–469 · DOI
  43. Yoshimoto K, Hanaoka H, Sato S, Kato T, Tabata S, Noda T, Ohsumi Y (2004) Processing of ATG8s, ubiquitin-like proteins, and their deconjugation by ATG4s are essential for plant autophagy. Plant Cell16:2967–2983 · DOI · Paper page

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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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CoChat. (2026). Citation check: Autophagic Nutrient Recycling in Arabidopsis Directed by the ATG8 and ATG12 Conjugation Pathways. https://app.cochat.ai/papers/10.1104/pp.105.060673
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Thompson, A. R., Doelling, J. H., Suttangkakul, A., & Vierstra, R. D. (2005). Autophagic Nutrient Recycling in Arabidopsis Directed by the ATG8 and ATG12 Conjugation Pathways. Plant Physiology. https://doi.org/10.1104/pp.105.060673