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Dual and dynamic intracellular localization of Arabidopsis thaliana SnRK1.1.
Blanco, Nicolás E; Liebsch, Daniela; Guinea Díaz, Manuel; Strand, Åsa; Whelan, James.
Afiliação
  • Blanco NE; Centro de Estudios Fotosintéticos y Bioquímicos, Universidad Nacional de Rosario (CEFOBI-CONICET/UNR), Rosario, Argentina.
  • Liebsch D; Umeå Plant Science Centre, Department of Plant Physiologyogy, Umeå University, Sweden.
  • Guinea Díaz M; Umeå Plant Science Centre, Department of Plant Physiologyogy, Umeå University, Sweden.
  • Strand Å; Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Rosario, Argentina.
  • Whelan J; Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.
J Exp Bot ; 70(8): 2325-2338, 2019 04 15.
Article em En | MEDLINE | ID: mdl-30753728
ABSTRACT
Sucrose non-fermenting 1 (SNF1)-related protein kinase 1.1 (SnRK1.1; also known as KIN10 or SnRK1α) has been identified as the catalytic subunit of the complex SnRK1, the Arabidopsis thaliana homologue of a central integrator of energy and stress signalling in eukaryotes dubbed AMPK/Snf1/SnRK1. A nuclear localization of SnRK1.1 has been previously described and is in line with its function as an integrator of energy and stress signals. Here, using two biological models (Nicotiana benthamiana and Arabidopsis thaliana), native regulatory sequences, different microscopy techniques, and manipulations of cellular energy status, it was found that SnRK1.1 is localized dynamically between the nucleus and endoplasmic reticulum (ER). This distribution was confirmed at a spatial and temporal level by co-localization studies with two different fluorescent ER markers, one of them being the SnRK1.1 phosphorylation target HMGR. The ER and nuclear localization displayed a dynamic behaviour in response to perturbations of the plastidic electron transport chain. These results suggest that an ER-associated SnRK1.1 fraction might be sensing the cellular energy status, being a point of crosstalk with other ER stress regulatory pathways.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Núcleo Celular / Proteínas Serina-Treonina Quinases / Arabidopsis / Proteínas de Arabidopsis / Retículo Endoplasmático Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Núcleo Celular / Proteínas Serina-Treonina Quinases / Arabidopsis / Proteínas de Arabidopsis / Retículo Endoplasmático Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 2019 Tipo de documento: Article