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Dual and dynamic intracellular localization of Arabidopsis thaliana SnRK1.1
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). Centro de Estudios Fotosintéticos y Bioquímicos, Universidad Nacional de Rosario (CEFOBI-CONICET/UNR), Rosario, Argentina.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Rosario, Argentina.ORCID iD: 0000-0003-2457-7376
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0001-6664-0471
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2019 (English)In: Journal of Experimental Botany, ISSN 0022-0957, E-ISSN 1460-2431, Vol. 70, no 8, p. 2325-2338Article in journal (Refereed) Published
Abstract [en]

Sucrose non-fermenting 1 (SNF1)-related protein kinase 1.1 (SnRK1.1; also known as KIN10 or SnRK1 alpha) 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.

Place, publisher, year, edition, pages
Oxford University Press, 2019. Vol. 70, no 8, p. 2325-2338
Keywords [en]
Arabidopsis, chloroplast, dual localization, endoplasmic reticulum (ER), ER localization, energy atus, Nicotiana benthamiana, nuclear localization, retrograde signalling, SnRK1.1
National Category
Cell Biology
Identifiers
URN: urn:nbn:se:umu:diva-163707DOI: 10.1093/jxb/erz023ISI: 000483170800010PubMedID: 30753728OAI: oai:DiVA.org:umu-163707DiVA, id: diva2:1361623
Available from: 2019-10-16 Created: 2019-10-16 Last updated: 2019-10-16Bibliographically approved

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Blanco, Nicolas E.Liebsch, DanielaStrand, Åsa

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Blanco, Nicolas E.Liebsch, DanielaGuinea Diaz, ManuelStrand, ÅsaWhelan, James
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