Proteomics

Dataset Information

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Function of constitutively active AtCPK1


ABSTRACT: One of the main Ca2+ decoders in plants are calcium-dependent protein kinases (CDPKs). Among them, AtCPK1 is one of the best studied as a positive regulator in the plant response to biotic and abiotic stress. Inactivation of the autoinhibitory domain of AtCPK1 (the mutated form of AtCPK1-Ca) provides constitutive activity of the kinase via imitation of the stress-induced Ca2+ increase. For the first time in the present study, we performed a proteomic analysis of the overexpressed mutant AtCPK1-Ca form of Arabidopsis thaliana in transformed Vitis amurensis calli. In our previous studies, we have shown that overexpression of this mutated form led to dramatically enhanced specialised metabolism in plant cell cultures, including resveratrol in V. amurensis.

INSTRUMENT(S): autoflex

ORGANISM(S): Vitis Amurensis

TISSUE(S): Cell Culture

SUBMITTER: Dmitriy Bulgakov  

LAB HEAD: Dr Victor P. Bulgakov

PROVIDER: PXD043507 | Pride | 2023-10-24

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
Annexin.fasta Fasta
Annexin_33595-8.31-biotools.mgf Mgf
Annexin_33595-8.31-flex.mzXML Mzxml
Annexin_33595-8.31-mascot.dat Other
Annexin_33595-8.31_1.1-SwissProt.mzid.gz Mzid
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Publications

Proteome-Level Investigation of <i>Vitis amurensis</i> Calli Transformed with a Constitutively Active, Ca<sup>2+</sup>-Independent Form of the <i>Arabidopsis AtCPK1</i> Gene.

Veremeichik Galina N GN   Bulgakov Dmitry V DV   Konnova Yuliya A YA   Brodovskaya Evgenia V EV   Grigorchuk Valeria P VP   Bulgakov Victor P VP  

International journal of molecular sciences 20230824 17


Calcium-dependent protein kinases (CDPKs) are one of the main Ca<sup>2+</sup> decoders in plants. Among them, <i>Arabidopsis thaliana AtCPK1</i> is one of the most studied CDPK genes as a positive regulator of plant responses to biotic and abiotic stress. The mutated form of <i>AtCPK1</i>, in which the autoinhibitory domain is inactivated (<i>AtCPK1-Ca</i>), provides constitutive kinase activity by mimicking a stress-induced increase in the Ca<sup>2+</sup> flux. In the present study, we performe  ...[more]

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