Proteomics

Dataset Information

0

Post-translational modification mapping - CRK10 WT and crk10-A397T kinase domain


ABSTRACT: We have analysed the recombinant kinase domain of AtCRK10 (At4g23180) purified as an N-terminal His-tag from Escherichia coli cells by LC-MS/MS. Both the WT and the crk10-A39T7 mutant allele of the CRK10 kinase domain were analysed. Post-translational modifications were identified, and a MASCOT search was carried out.

INSTRUMENT(S): Q Exactive HF

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

SUBMITTER: Maiara Piovesana  

LAB HEAD: Michaela Matthes

PROVIDER: PXD023831 | Pride | 2023-07-20

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
F006340_Mutant.dat Other
F006341_WT.dat Other
P736_Mutant.mht Other
P736_Mutant.raw Raw
P736_WT.mht Other
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Publications

A point mutation in the kinase domain of CRK10 leads to xylem vessel collapse and activation of defence responses in Arabidopsis.

Piovesana Maiara M   Wood Ana K M AKM   Smith Daniel P DP   Deery Michael J MJ   Bayliss Richard R   Carrera Esther E   Wellner Nikolaus N   Kosik Ondrej O   Napier Johnathan A JA   Kurup Smita S   Matthes Michaela C MC  

Journal of experimental botany 20230501 10


Cysteine-rich receptor-like kinases (CRKs) are a large family of plasma membrane-bound receptors ubiquitous in higher plants. However, despite their prominence, their biological roles have remained largely elusive so far. In this study we report the characterization of an Arabidopsis mutant named crk10-A397T in which alanine 397 has been replaced by a threonine in the αC helix of the kinase domain of CRK10, known to be a crucial regulatory module in mammalian kinases. The crk10-A397T mutant is a  ...[more]

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