LARDON, Robin, Hoang Khai TRINH, Xiangyu XU, Lam Dai VU, Brigitte VAN DE COTTE, Markéta PERNISOVÁ, Steffen VANNESTE, Ive DE SMET and Danny GEELEN. Histidine kinase inhibitors impair shoot regeneration in Arabidopsis thaliana via cytokinin signaling and SAM patterning determinants. Frontiers in Plant Science. Frontiers Media S.A., 2022, vol. 13, September, p. 1-22. ISSN 1664-462X. Available from: https://dx.doi.org/10.3389/fpls.2022.894208.
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Basic information
Original name Histidine kinase inhibitors impair shoot regeneration in Arabidopsis thaliana via cytokinin signaling and SAM patterning determinants
Authors LARDON, Robin, Hoang Khai TRINH, Xiangyu XU, Lam Dai VU, Brigitte VAN DE COTTE, Markéta PERNISOVÁ (203 Czech Republic, guarantor, belonging to the institution), Steffen VANNESTE, Ive DE SMET and Danny GEELEN.
Edition Frontiers in Plant Science, Frontiers Media S.A. 2022, 1664-462X.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Switzerland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 5.600
RIV identification code RIV/00216224:14310/22:00126910
Organization unit Faculty of Science
Doi http://dx.doi.org/10.3389/fpls.2022.894208
UT WoS 000871680800001
Keywords in English phosphoproteomics; kinase inhibitors; cytokinin signaling; shoot regeneration; organogenesis
Tags CF PLANT, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Marie Šípková, DiS., učo 437722. Changed: 18/1/2023 11:14.
Abstract
Reversible protein phosphorylation is a post-translational modification involved in virtually all plant processes, as it mediates protein activity and signal transduction. Here, we probe dynamic protein phosphorylation during de novo shoot organogenesis in Arabidopsis thaliana. We find that application of three kinase inhibitors in various time intervals has different effects on root explants. Short exposures to the putative histidine (His) kinase inhibitor TCSA during the initial days on shoot induction medium (SIM) are detrimental for regeneration in seven natural accessions. Investigation of cytokinin signaling mutants, as well as reporter lines for hormone responses and shoot markers, suggests that TCSA impedes cytokinin signal transduction via AHK3, AHK4, AHP3, and AHP5. A mass spectrometry-based phosphoproteome analysis further reveals profound deregulation of Ser/Thr/Tyr phosphoproteins regulating protein modification, transcription, vesicle trafficking, organ morphogenesis, and cation transport. Among TCSA-responsive factors are prior candidates with a role in shoot apical meristem patterning, such as AGO1, BAM1, PLL5, FIP37, TOP1ALPHA, and RBR1, as well as proteins involved in polar auxin transport (e.g., PIN1) and brassinosteroid signaling (e.g., BIN2). Putative novel regeneration determinants regulated by TCSA include RD2, AT1G52780, PVA11, and AVT1C, while NAIP2, OPS, ARR1, QKY, and aquaporins exhibit differential phospholevels on control SIM. LC–MS/MS data are available via ProteomeXchange with identifier PXD030754.
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