Your browser doesn't support javascript.
loading
Arabidopsis ROOT PHOTOTROPISM2 Is a Light-Dependent Dynamic Modulator of Phototropin1.
Kimura, Taro; Tsuchida-Mayama, Tomoko; Imai, Hirotatsu; Okajima, Koji; Ito, Kosuke; Sakai, Tatsuya.
Afiliação
  • Kimura T; Graduate School of Science and Technology, Niigata University, Niigata-shi, Niigata, 950-2181, Japan.
  • Tsuchida-Mayama T; RIKEN Plant Science Center, Yokohama, Kanagawa 230-0045, Japan.
  • Imai H; Graduate School of Science and Technology, Niigata University, Niigata-shi, Niigata, 950-2181, Japan.
  • Okajima K; Research Fellow of Japan Society for the Promotion of Science, Kojimachi Business Center Building, Chiyoda-ku, Tokyo 102-0083, Japan.
  • Ito K; Department of Physics, Keio University, 3-14-1, Hiyoshi, Kouhoku-ku, Yokohama, Kanagawa 223-8522, Japan.
  • Sakai T; Graduate School of Science and Technology, Niigata University, Niigata-shi, Niigata, 950-2181, Japan.
Plant Cell ; 32(6): 2004-2019, 2020 06.
Article em En | MEDLINE | ID: mdl-32213636
The Arabidopsis (Arabidopsis thaliana) blue light photoreceptor phototropin1 (phot1) is a blue light-activated Ser/Thr protein kinase that mediates various light responses, including phototropism. The function of phot1 in hypocotyl phototropism is dependent on the light induction of ROOT PHOTOTROPISM2 (RPT2) proteins within a broad range of blue light intensities. It is not yet known however how RPT2 contributes to the photosensory adaptation of phot1 to high intensity blue light and the phototropic responses under bright light conditions. We show that RPT2 suppresses the activity of phot1 and demonstrate that RPT2 binds to the PHOT1 light, oxygen or voltage sensing1 (LOV1) domain that is required for its high photosensitivity. Our biochemical analyses revealed that RPT2 inhibits autophosphorylation of phot1, suggesting that it suppresses the photosensitivity and/or kinase activity of phot1 through the inhibition of LOV1 function. We found that RPT2 proteins are degraded via a ubiquitin-proteasome pathway when phot1 is inactive and are stabilized under blue light in a phot1-dependent manner. We propose that RPT2 is a molecular rheostat that maintains a moderate activation level of phot1 under any light intensity conditions.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Plant Cell Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Plant Cell Ano de publicação: 2020 Tipo de documento: Article