Ubiquitination of the tomato cell death suppressor Adi3 by the RING E3 ubiquitin ligase AdBiL |
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| Authors: | Julian Avila Timothy P. Devarenne |
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| Affiliation: | 1. INRA-Theix, UMR1019, Unité de nutrition humaine, CRNH Auvergne, Université d''Auvergne Clermont-Ferrand, France;2. Inserm U954, Faculté de Médecine/CHU, Université Henri Poincaré, Nancy, France;1. Department of Oral Microbiology and Immunology, DRI, and BK21 Plus Program, School of Dentistry, Seoul National University, Seoul 110-749, Republic of Korea;2. Department of Agricultural Biotechnology and Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul 151-921, Republic of Korea;3. Laboratory Sciences Division, International Vaccine Institute, Seoul 151-742, Republic of Korea;1. Department of Pharmacology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030, USA;2. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 4 Kosygin Street, Moscow 119991, Russian Federation;1. Division of Cellular Immunology, Kitasato University Graduate School of Medical Science, Kitasato, 1-15-1, Minami-ku, Sagamihara, Kanagawa, 252-0373, Japan;2. Ehime Plant, Dainippon Sumitomo Pharma Co., Ltd., Sobiraki-cho, Niihama, Ehime, 792-0001, Japan;3. Department of Mechanical Engineering, Keio University, Hiyoshi 3-14-1, Kita, Kohoku-ku, Yokohama, Kanagawa, 223-8522, Japan;4. Department of Immunology, Juntendo University School of Medicine, Hongo 2-1-1, Bunkyo-ku, Tokyo 113-8421, Japan;5. Division of Fundamental Medical Technology, Department of Immunology, Ehime Prefecture University of Health Sciences, Takooda 543, Tobe-cho, Iyo-gun, Ehime, 791-2101, Japan;1. Department of Horticultural Biotechnology, Kyung Hee University, Yongin 446-701, Republic of Korea;2. Department of Plant Science, Seoul National University, Seoul 151-742, Republic of Korea;3. Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA;4. Department of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA |
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| Abstract: | Programmed cell death (PCD) is an organized process by which organisms selectively remove cells according to developmental needs or in response to biotic or abiotic stress. Despite recent efforts to understand mechanisms by which cell death takes place in plants, several gaps remain in our understanding of the molecular elements involved. The tomato PCD suppressor Adi3 is an AGC kinase that shares functional homology with the mammalian inhibitor of apoptosis PKB. Regulation of PKB stability, cell localization, and activation state is achieved through post-translational modifications such as ubiquitination. In an effort to understand the regulation of Adi3 function, we studied its interaction with the E3 ubiquitin ligase AdBiL. Using in vitro ubiquitination assays we show that AdBiL is an active E3 ubiquitin ligase using the E2 ubiquitin ligase UBC8 to ubiquitinate Adi3. Adi3 is also degraded in a proteasome-dependent manner. Our data draws additional parallels between Adi3 and PKB to support the functional relationship between these two PCD regulators. |
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