Proteomics

Dataset Information

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ACONITASE 3 is post-translationally controlled in response to mitochondrial stress signals in Arabidopsis


ABSTRACT: Mitochondria are tightly embedded within metabolic and regulatory networks that optimize plant performance upon environmental challenges. The best-known mitochondrial retrograde signaling pathway involves stress-induced activation of the transcription factor ANAC017, which mediates the onset of protective responses upon stress-induced mitochondrial dysfunction in Arabidopsis. Post-translational control of the elicited responses, in contrast, remains poorly understood. Previous studies linked protein phosphatase 2A subunit PP2A-B’γ, a key negative regulator of stress responses, with reversible phosphorylation of ACONITASE 3 (ACO3). Here we report on ACO3 and its phosphorylation at Ser91 as regulatory components induced by mitochondrial dysfunction. Targeted mass spectrometry-based proteomics revealed that the abundance and phosphorylation of ACO3 increased under stress, and that this required signaling through ANAC017. Phosphomimetic mutation at ACO3-Ser91 and the accumulation of ACO3S91D-YFP, in turn, promoted the expression of stress related genes and ACO3 function associated with plant tolerance against UV-B or antimycin A-induced mitochondrial dysfunction. These findings positioned ACO3 both as a target and modulator of mitochondrial dysfunction signaling, critical in the attainment of stress tolerance in Arabidopsis leaves.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Jesús Pascual  

LAB HEAD: Saijaliisa Kangasjärvi

PROVIDER: PXD024316 | Pride | 2021-06-08

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
ACO_UV_1.msf Msf
ACO_UV_1.mzML Mzml
ACO_UV_1.mzid.gz Mzid
ACO_UV_1.raw Raw
ACO_UV_2.msf Msf
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