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Shino Goto-Yamada - Polonez 2

Analysis of quality control of peroxisomes depending on chaperon, protease and autophagy

Polonez 2 - Project entitled: 

Analysis of quality control of peroxisomes depending on chaperon, protease and autophagy

Fellowship registration number: 2016/21/P/NZ9/01089



The quality control mechanism is necessary to the organellar and cellular homeostasis. In order to keep the cells to always-optimal state, organelles/cells quickly remove abnormal cellular components, such as proteins misfolded during their synthesis and damaged by exposure to stress (e.g. heat, UV, reactive oxygen species). This process is essential for survival of cells and organisms. Indeed, many human diseases are causally linked to misfolding and accumulation of proteins. We focus on one of the organelles, peroxisome, which is ubiquitously present in eukaryotic cells. Peroxisomes are essential for cell survival because they contains multiple metabolic systems such as fatty acid metabolism and, in plants, photorespiration. In these processes, hydrogen peroxide (H2O2) is generated inside peroxisomes, which is detoxified by the peroxisomal enzyme, catalase. However, some part of H2O2 harmful to peroxisomal proteins and ultimately peroxisomes become dysfunctional. Therefore, a quality control system that removes unnecessary, abnormal and toxic peroxisomal proteins or peroxisomes is important for maintaining the optimal performance of peroxisomes. Recently we have revealed that the balance between a LON protease function and autophagy is important for the peroxisome homeostasis. This project focuses on understanding the molecular mechanism how the peroxisomal quality is controlled by the protease and autophagy.

Aims of the project:

Understanding of the suppression mechanism of pexophagy by the LON protease. 
Identification of a protein linking peroxisomes and autophagy.
Isolation of novel autophagy-related genes in plants. 

Education & Experience:

2017–present: POLONEZ fellowship from the National Science Centre co-funded from the EU H2020 Marie Skłodowska-Curie Actions, Malopolska Centre of Biotechnology (MCB), Jagiellonian University, Krakow, Poland.
2015–2017: Research Fellowship from the Japan Society for the Promotion of Science, affiliated with Graduate School of Science, Kyoto University, Kyoto, Japan.
2014–2015: Postdoctoral fellow in Graduate School of Science, Kyoto University, Kyoto, Japan.
2012–2014: NIBB Research Fellow, National Institute for Basic Biology (NIBB), Aichi, Japan
2011: PhD in Science, National Institute for Basic Biology, affiliated with School of Life Science, The Graduate University for Advanced Studies, Aichi, Japan.
2010–2012: Research Fellowship from the Japan Society for the Promotion of Science, affiliated with National Institute for Basic Biology, Aichi, Japan


1. Kamigaki, A., Nito, K., Hikino, K., Goto-Yamada, S., Nishimura, M., Nakagawa, T., et al. (2016) Gateway vectors for simultaneous detection of multiple protein-protein interactions in plant cells using bimolecular fluorescence complementation. PLoS One 11: e0160717.
2. Goto-Yamada, S., Mano, S., Yamada, K., Oikawa, K., Hosokawa, Y., Hara-Nishimura, I., and Nishimura, M. (2015). Dynamics of the light-dependent transition of plant peroxisomes. Plant Cell Physiol. 56, 1264-1271.
3. Hatsugai, N., Yamada, K., Goto-Yamada, S., and Hara-Nishimura, I. (2015). Vacuolar processing enzyme in plant programmed cell death. Front. Plant Sci. 6, 234.
4. Goto-Yamada, S., Mano, S., Oikawa, K., Shibata, M., and Nishimura, M. (2014). Interaction between chaperone and protease functions of LON2, and autophagy during the functional transition of peroxisomes. Plant Sig. Behav. 9, e28838.
5. Shibata, M., Oikawa, K., Yoshimoto, K., Goto-Yamada, S., Mano, S., Yamada, K., Kondo, M., Hayashi, M., Sakamoto, W., Ohsumi, Y., et al. (2014). Plant autophagy is responsible for peroxisomal transition and plays an important role in the maintenance of peroxisomal quality. Autophagy 10, 936-937.
6. Goto-Yamada, S., Mano, S., Nakamori, C., Kondo, M., Yamawaki, R., Kato, A., and Nishimura, M. (2014). Chaperone and protease functions of LON protease 2 modulate the peroxisomal transition and degradation with autophagy. Plant Cell Physiol. 55, 482-496.
7. Goto-Yamada, S., Mano, S., and Nishimura, M. (2014). The role of peroxisomes in plant reproductive processes. In Sexual reproduction in animals and plants, H. Sawada, N. Inoue and M. Iwano, eds. (Springer Japan), pp. pp 419-429.
8. Tanaka, Y., Kimura, T., Hikino, K., Goto, S., Nishimura, M., Mano, S., and Nakagawa, T. (2012). Gateway vectors for plant genetic engineering: overview of plant vectors, application for bimolecular fluorescence complementation (BiFC) and multigene construction. In Genetic Engineering - Basics, New Applications and Responsibilities, H.A. Barrera-Saldaña, ed. (InTech), pp. 35-58.
9. Goto, S., Mano, S., Nakamori, C., and Nishimura, M. (2011). Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the PEX1-PEX6 complex to peroxisomes. Plant Cell 23, 1573-1587.
10. Singh, T., Hayashi, M., Mano, S., Arai, Y., Goto, S., and Nishimura, M. (2009). Molecular components required for the targeting of PEX7 to peroxisomes in Arabidopsis thaliana. Plant J. 60, 488-498.






This project has received funding from the European Union’s Horizon 2020 research and innovation programme under the Marie Skłodowska-Curie grant agreement No. 665778