Highly Oxidized Peroxisomes Are Selectively Degraded via Autophagy in Arabidopsisстатья из журнала
Аннотация: The positioning of peroxisomes in a cell is a regulated process that is closely associated with their functions. Using this feature of the peroxisomal positioning as a criterion, we identified three Arabidopsis thaliana mutants (peroxisome unusual positioning1 [peup1], peup2, and peup4) that contain aggregated peroxisomes. We found that the PEUP1, PEUP2, and PEUP4 were identical to Autophagy-related2 (ATG2), ATG18a, and ATG7, respectively, which are involved in the autophagic system. The number of peroxisomes was increased and the peroxisomal proteins were highly accumulated in the peup1 mutant, suggesting that peroxisome degradation by autophagy (pexophagy) is deficient in the peup1 mutant. These aggregated peroxisomes contained high levels of inactive catalase and were more oxidative than those of the wild type, indicating that peroxisome aggregates comprise damaged peroxisomes. In addition, peroxisome aggregation was induced in wild-type plants by exogenous application of hydrogen peroxide. The cat2 mutant also contained peroxisome aggregates. These findings demonstrate that hydrogen peroxide as a result of catalase inactivation is the inducer of peroxisome aggregation. Furthermore, an autophagosome marker, ATG8, frequently colocalized with peroxisome aggregates, indicating that peroxisomes damaged by hydrogen peroxide are selectively degraded by autophagy in the wild type. Our data provide evidence that autophagy is crucial for quality control mechanisms for peroxisomes in Arabidopsis.
Год издания: 2013
Авторы: Michitaro Shibata, Kazusato Oikawa, Kohki Yoshimoto, Maki Kondo, Shoji Mano, Kenji Yamada, Makoto Hayashi, Wataru Sakamoto, Yoshinori Ohsumi, Mikio Nishimura
Издательство: Oxford University Press
Источник: The Plant Cell
Ключевые слова: Autophagy in Disease and Therapy, Peroxisome Proliferator-Activated Receptors, Lipid metabolism and biosynthesis
Другие ссылки: The Plant Cell (HTML)
HAL (Le Centre pour la Communication Scientifique Directe) (HTML)
PubMed Central (HTML)
PubMed (HTML)
HAL (Le Centre pour la Communication Scientifique Directe) (HTML)
PubMed Central (HTML)
PubMed (HTML)
Открытый доступ: bronze
Том: 25
Выпуск: 12
Страницы: 4967–4983