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231226s2022 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erac315
|2 doi
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|a DE-627
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|e rakwb
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|a eng
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|a Gutierrez-Beltran, Emilio
|e verfasserin
|4 aut
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|a Compartmentalization, a key mechanism controlling the multitasking role of the SnRK1 complex
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|c 2022
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|a Text
|b txt
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 16.11.2022
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|a Date Revised 22.11.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author(s) 2022. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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|a SNF1-related protein kinase 1 (SnRK1), the plant ortholog of mammalian AMP-activated protein kinase/fungal (yeast) Sucrose Non-Fermenting 1 (AMPK/SNF1), plays a central role in metabolic responses to reduced energy levels in response to nutritional and environmental stresses. SnRK1 functions as a heterotrimeric complex composed of a catalytic α- and regulatory β- and βγ-subunits. SnRK1 is a multitasking protein involved in regulating various cellular functions, including growth, autophagy, stress response, stomatal development, pollen maturation, hormone signaling, and gene expression. However, little is known about the mechanism whereby SnRK1 ensures differential execution of downstream functions. Compartmentalization has been recently proposed as a new key mechanism for regulating SnRK1 signaling in response to stimuli. In this review, we discuss the multitasking role of SnRK1 signaling associated with different subcellular compartments
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|a Review
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Autophagy
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|a SnRK1 compartmentalization
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|a SnRK1-interacting proteins
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|a SnRK1/TOR signaling
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|a plant cell
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|a stress granules
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|a AMP-Activated Protein Kinases
|2 NLM
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|a EC 2.7.11.31
|2 NLM
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|a Arabidopsis Proteins
|2 NLM
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|a Crespo, Jose L
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 73(2022), 20 vom: 15. Nov., Seite 7055-7067
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnas
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|g volume:73
|g year:2022
|g number:20
|g day:15
|g month:11
|g pages:7055-7067
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|u http://dx.doi.org/10.1093/jxb/erac315
|3 Volltext
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