Effects of tyrosine kinase and phosphatase inhibitors on mitosis progression in synchronized tobacco BY-2 cells

Sheremet, Ya. A.; Yemets, А. І.; Azmi, Asfar S.; Vissenberg, Kris; Verbelen, Jean‐Pierre; Blume, Ya. B.

doi:10.3103/s0095452712050088

Cited by 7 publications

(9 citation statements)

References 45 publications

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“…3a ) is known as an inhibitor of mammalian PTKs 15 , the target of GNS in plants is unknown. Furthermore, several studies have shown that Tyr residues of beta-tubulins are phosphorylated in plants 28 , and GNS and Tyr-phosphatase inhibitors affect microtubule organization 29 , 30 . In our previous study, we reported that Tyr residues of beta-tubulin 2 and 7 were phosphorylated by CRK2 and CRK3 in plants 22 .…”

Section: Resultsmentioning

confidence: 99%

Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation

et al. 2017

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Gibberellin (GA) is a major hormone for plant growth and development. GA response is derived from the degradation of DELLA repressor proteins after GA-dependent complex formation of the GID1 GA receptor with DELLA. Genistein is a known tyrosine (Tyr) kinase inhibitor and inhibits DELLA degradation. However, the biological role of Tyr phosphorylation on the GA response remains unclear. Here, we demonstrate that GARU (GA receptor RING E3 ubiquitin ligase) mediates ubiquitin-dependent degradation of GID1, and that the TAGK2 plant Tyr-kinase is a target of genistein and inhibits GARU–GID1A interactions by phosphorylation of GARU at Tyr321. Genistein induces degradation of GID1 and accumulation of DELLA. Conversely, Arabidopsis garu mutant and TAGK2-overexpressing plants accelerate GID1 stabilization and DELLA degradation. Under salt stress, GARU suppresses seed germination. We propose that GA response is negatively regulated by GARU-dependent GID1 ubiquitination and positively by Tyr phosphorylation of GARU by TAGK2, and genistein inhibits GA signaling by TAGK2 inhibition.

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Section: Resultsmentioning

confidence: 99%

Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation

et al. 2017

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“…In addition, meta-analysis of phosphoproteomic data revealed that Tyr-phosphorylated peptides are overrepresented in mitochondrial and characterized two Tyr phosphorylation motifs (6). Other studies have demonstrated that PTK and PTP inhibitor application to plants alter abscisic acid (8), gibberellin (9), cold stress (10), and sugar responses (11), as well as cytoskeleton organization (12) and cell division (13). These findings strongly suggest that plants possess Tyr phosphorylation signaling pathways.…”

Section: Tyrmentioning

confidence: 88%

“…Our results strongly suggest that CRKs are the responsible kinases for the Tyr phosphorylation of TBBs. Pharmacological approaches showed that PTK and PTP inhibitors can alter the stability and orientation of the microtubules (MTs) (12,13). In mammals, membrane-associated TBBs were phosphorylated by membrane-associated pp60c-src in nerve growth cones membranes (53).…”

Section: Discussionmentioning

confidence: 99%

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Nemoto

Takemori

Seki

et al. 2015

Journal of Biological Chemistry

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Background: Protein kinases that catalyze Tyr phosphorylation in plants in vivo are largely unknown. Results: CDPK/CPK-related protein kinases (CRKs) that auto/trans-phosphorylate Tyr residues and six substrates of these were identified. CRK knock-out mutants show reduced Tyr phosphorylation of ␤-tubulin proteins. Conclusion: CRKs can phosphorylate Tyr residues of ␤-tubulin and certain transcription factors. Significance: CRKs might be responsible for much of the protein Tyr phosphorylation in vivo.

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“…It is likely that tubulin phosphorylation detected herein, corresponds to Thr-349 as previously reported (Ban et al, 2013 ). However, α-tubulin might be also targeted for Tyr phosphorylation regulating microtubule sensitivity to low temperatures (Sheremet et al, 2012a ), growth and morphogenesis of Arabidopsis root cells (Yemets et al, 2008 ) and mitotic progression in dividing tobacco BY-2 suspension culture cells (Sheremet et al, 2012b ). Although, the identity of phosphorylated residues in tubulin (and any other protein) cannot be revealed by Phos-Tag™, the method can be readily combined with immunoprecipitation of the protein of interest and subsequent probing of the resulting western blot with phospho-amino acid specific antibodies.…”

Section: Importance Of Post-electrophoretic Processing Of the Gelmentioning

confidence: 99%

Monitoring protein phosphorylation by acrylamide pendant Phos-Tagâ„¢ in various plants

et al. 2015

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The aim of the present study is to rationalize acrylamide pendant Phos-Tag™ in-gel discrimination of phosphorylated and non-phosphorylated plant protein species with standard immunoblot analysis, and optimize sample preparation, efficient electrophoretic separation and transfer. We tested variants of the method including extraction buffers suitable for preservation of phosphorylated protein species in crude extracts from plants and we addressed the importance of the cation (Mn2+ or Zn2+) used in the gel recipe for efficient transfer to PVDF membranes for further immunoblot analysis. We demonstrate the monitoring of Medicago sativa stress-induced mitogen activated protein kinase (SIMK) in stress-treated wild type plants and transgenic SIMKK RNAi line. We further show the hyperosmotically-induced phosphorylation of the previously uncharacterized HvMPK4 of barley. The method is validated using inducible phosphorylation of barley and wheat α-tubulin and of Arabidopsis MPK6. Acrylamide pendant Phos-Tag™offers a flexible tool for studying protein phosphorylation in crops and Arabidopsis circumventing radioactive labeling and the use of phosphorylation specific antibodies.

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Effects of tyrosine kinase and phosphatase inhibitors on mitosis progression in synchronized tobacco BY-2 cells

Abstract: To test whether reversible tubulin phosphorylation plays any role in the process of plant mitosis the effects of inhibitors of tyrosine kinases, herbimycin

Cited by 7 publications

References 45 publications

Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation

Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation

Members of the Plant CRK Superfamily Are Capable of Trans- and Autophosphorylation of Tyrosine Residues

Monitoring protein phosphorylation by acrylamide pendant Phos-Tagâ„¢ in various plants

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