In plants, sucrose nonfermenting 1 (SNF1)-related protein kinase 1 (SnRK1) is a key energy-sensor that orchestrates large-scale transcriptional reprogramming to maintain cellular homeostasis under energy deficit. SnRK1 activity is under tight negative control, although the exact mechanisms leading to its activation are not well understood. We show that the Arabidopsis (Arabidopsis thaliana) DOMAIN OF UNKNOWN FUNCTION (DUF581) protein DUF581-9/FCS-like zinc finger (FLZ) 3 binds to the catalytic SnRK1.1 alpha subunit (KIN10) to inhibit its activation by geminivirus rep-interacting kinase (GRIK)-dependent T-loop phosphorylation. Overexpression of DUF581-9 in Arabidopsis dampens SnRK1 signalling and interferes with adaptation to dark-induced starvation. The presence of DUF581-9 significantly reduced SnRK1 activity in protoplasts and in vitro. This was accompanied by a reduction in T175 T-loop phosphorylation and also diminished KIN10 auto-phosphorylation. Furthermore, DUF581-9 reduced binding of the up-stream activating kinase GRIK2 to KIN10, explaining the reduced KIN10 T-loop phosphorylation. Ectopically expressed DUF581-9 protein was rapidly turned over by the proteasome when Arabidopsis plants were subjected to starvation treatment, likely releasing its inhibitory activity on the SnRK1 complex. Taken together, our results support a model in which DUF581-9 negatively regulates SnRK1 activity under energy sufficient conditions. Turnover of the protein provides a rapid way for SnRK1 activation under energy deficit without the need of de novo protein synthesis.
Bortlik, Jennifer
Luhle, Jost
Alseekh, Saleh
Weiste, Christoph
Fernie, Alisdair R
Droge-Laser, Wolfgang
Bornke, Frederik
eng
2023/11/08
Plant Physiol. 2023 Nov 4:kiad594. doi: 10.1093/plphys/kiad594.
%0 Journal Article
%1 bortlik2023domain
%A Bortlik, J.
%A Luhle, J.
%A Alseekh, S.
%A Weiste, C.
%A Fernie, A. R.
%A Droge-Laser, W.
%A Bornke, F.
%D 2023
%J Plant Physiol
%K imported myOwn
%R 10.1093/plphys/kiad594
%T DOMAIN OF UNKNOWN FUNCTION581-9 negatively regulates SnRK1 kinase activity
%U https://www.ncbi.nlm.nih.gov/pubmed/37936321
%X In plants, sucrose nonfermenting 1 (SNF1)-related protein kinase 1 (SnRK1) is a key energy-sensor that orchestrates large-scale transcriptional reprogramming to maintain cellular homeostasis under energy deficit. SnRK1 activity is under tight negative control, although the exact mechanisms leading to its activation are not well understood. We show that the Arabidopsis (Arabidopsis thaliana) DOMAIN OF UNKNOWN FUNCTION (DUF581) protein DUF581-9/FCS-like zinc finger (FLZ) 3 binds to the catalytic SnRK1.1 alpha subunit (KIN10) to inhibit its activation by geminivirus rep-interacting kinase (GRIK)-dependent T-loop phosphorylation. Overexpression of DUF581-9 in Arabidopsis dampens SnRK1 signalling and interferes with adaptation to dark-induced starvation. The presence of DUF581-9 significantly reduced SnRK1 activity in protoplasts and in vitro. This was accompanied by a reduction in T175 T-loop phosphorylation and also diminished KIN10 auto-phosphorylation. Furthermore, DUF581-9 reduced binding of the up-stream activating kinase GRIK2 to KIN10, explaining the reduced KIN10 T-loop phosphorylation. Ectopically expressed DUF581-9 protein was rapidly turned over by the proteasome when Arabidopsis plants were subjected to starvation treatment, likely releasing its inhibitory activity on the SnRK1 complex. Taken together, our results support a model in which DUF581-9 negatively regulates SnRK1 activity under energy sufficient conditions. Turnover of the protein provides a rapid way for SnRK1 activation under energy deficit without the need of de novo protein synthesis.
@article{bortlik2023domain,
abstract = {In plants, sucrose nonfermenting 1 (SNF1)-related protein kinase 1 (SnRK1) is a key energy-sensor that orchestrates large-scale transcriptional reprogramming to maintain cellular homeostasis under energy deficit. SnRK1 activity is under tight negative control, although the exact mechanisms leading to its activation are not well understood. We show that the Arabidopsis (Arabidopsis thaliana) DOMAIN OF UNKNOWN FUNCTION (DUF581) protein DUF581-9/FCS-like zinc finger (FLZ) 3 binds to the catalytic SnRK1.1 alpha subunit (KIN10) to inhibit its activation by geminivirus rep-interacting kinase (GRIK)-dependent T-loop phosphorylation. Overexpression of DUF581-9 in Arabidopsis dampens SnRK1 signalling and interferes with adaptation to dark-induced starvation. The presence of DUF581-9 significantly reduced SnRK1 activity in protoplasts and in vitro. This was accompanied by a reduction in T175 T-loop phosphorylation and also diminished KIN10 auto-phosphorylation. Furthermore, DUF581-9 reduced binding of the up-stream activating kinase GRIK2 to KIN10, explaining the reduced KIN10 T-loop phosphorylation. Ectopically expressed DUF581-9 protein was rapidly turned over by the proteasome when Arabidopsis plants were subjected to starvation treatment, likely releasing its inhibitory activity on the SnRK1 complex. Taken together, our results support a model in which DUF581-9 negatively regulates SnRK1 activity under energy sufficient conditions. Turnover of the protein provides a rapid way for SnRK1 activation under energy deficit without the need of de novo protein synthesis.},
added-at = {2024-02-15T15:08:22.000+0100},
author = {Bortlik, J. and Luhle, J. and Alseekh, S. and Weiste, C. and Fernie, A. R. and Droge-Laser, W. and Bornke, F.},
biburl = {https://www.bibsonomy.org/bibtex/217767596a5958b2dfae5c313b6b54602/jvsi_all},
doi = {10.1093/plphys/kiad594},
interhash = {29080f14f67ee1bf64d58048e48de4a8},
intrahash = {17767596a5958b2dfae5c313b6b54602},
issn = {1532-2548 (Electronic)
0032-0889 (Linking)},
journal = {Plant Physiol},
keywords = {imported myOwn},
note = {Bortlik, Jennifer
Luhle, Jost
Alseekh, Saleh
Weiste, Christoph
Fernie, Alisdair R
Droge-Laser, Wolfgang
Bornke, Frederik
eng
2023/11/08
Plant Physiol. 2023 Nov 4:kiad594. doi: 10.1093/plphys/kiad594.},
timestamp = {2024-02-15T15:08:22.000+0100},
title = {DOMAIN OF UNKNOWN FUNCTION581-9 negatively regulates SnRK1 kinase activity},
type = {Journal Article},
url = {https://www.ncbi.nlm.nih.gov/pubmed/37936321},
year = 2023
}