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Dual and dynamic intracellular localization of Arabidopsis thaliana SnRK1.1.

Identifieur interne : 000179 ( Main/Exploration ); précédent : 000178; suivant : 000180

Dual and dynamic intracellular localization of Arabidopsis thaliana SnRK1.1.

Auteurs : Nicolás E. Blanco [Argentine, Suède] ; Daniela Liebsch [Suède, Argentine] ; Manuel Guinea Díaz [Finlande] ; Sa Strand [Suède] ; James Whelan [Australie]

Source :

RBID : pubmed:30753728

Descripteurs français

English descriptors

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.

DOI: 10.1093/jxb/erz023
PubMed: 30753728


Affiliations:


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<div type="abstract" xml:lang="en">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.</div>
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<Keyword MajorTopicYN="Y">Nicotiana benthamiana </Keyword>
<Keyword MajorTopicYN="Y">Arabidopsis</Keyword>
<Keyword MajorTopicYN="Y">ER localization</Keyword>
<Keyword MajorTopicYN="Y">SnRK1.1</Keyword>
<Keyword MajorTopicYN="Y">chloroplast</Keyword>
<Keyword MajorTopicYN="Y">dual localization</Keyword>
<Keyword MajorTopicYN="Y">endoplasmic reticulum (ER)</Keyword>
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<Keyword MajorTopicYN="Y">nuclear localization, retrograde signalling</Keyword>
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<li>Argentine</li>
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<li>Finlande occidentale</li>
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