A heat‐activated MAP kinase in tomato: a possible regulator of the heat stress response

Link, Vinzenz; Sinha, Alok; Vashista, Pooja; Hofmann, Markus; Proels, Reinhard K.; Ehneß, Rainer; Roitsch, Thomas

doi:10.1016/s0014-5793(02)03498-1

Cited by 71 publications

(62 citation statements)

References 43 publications

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“…Phosphorylation of heat shock factors by MAP kinases was reported in several organisms, including mammalian cells (Chu et al, 1996;Kim et al, 1997;Chen et al, 2001), yeast (Hashikawa and Sakurai, 2004), and plants (Link et al, 2002;Evrard et al, 2013). While phosphorylation repressed HSF1-dependent transcriptional activation in human cells (Chu et al, 1996), multimerisation of yeast HSF in connection with hyperphosphorylation enhanced induction of target genes (Hashikawa and Sakurai, 2004).…”

Section: Phosphorylation Of Hsfa4a By Interacting Mpk3 and Mpk6 Kinasesmentioning

confidence: 97%

“…While phosphorylation repressed HSF1-dependent transcriptional activation in human cells (Chu et al, 1996), multimerisation of yeast HSF in connection with hyperphosphorylation enhanced induction of target genes (Hashikawa and Sakurai, 2004). Heat-activated MAP kinases were shown to transduce heat stress signals by phosphorylating HSFs in tomato or promoting HSP gene expression in tobacco (Link et al, 2002;Suri and Dhindsa, 2008). Recently, phosphorylation and activation of Arabidopsis HSFA2 by MPK6 was reported (Evrard et al, 2013).…”

Section: Phosphorylation Of Hsfa4a By Interacting Mpk3 and Mpk6 Kinasesmentioning

confidence: 99%

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The Heat Shock Factor A4A Confers Salt Tolerance and Is Regulated by Oxidative Stress and the Mitogen-Activated Protein Kinases MPK3 and MPK6

et al. 2014

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Heat shock factors (HSFs) are principal regulators of plant responses to several abiotic stresses. Here, we show that estradioldependent induction of HSFA4A confers enhanced tolerance to salt and oxidative agents, whereas inactivation of HSFA4A results in hypersensitivity to salt stress in Arabidopsis (Arabidopsis thaliana). Estradiol induction of HSFA4A in transgenic plants decreases, while the knockout hsfa4a mutation elevates hydrogen peroxide accumulation and lipid peroxidation. Overexpression of HSFA4A alters the transcription of a large set of genes regulated by oxidative stress. In yeast (Saccharomyces cerevisiae) two-hybrid and bimolecular fluorescence complementation assays, HSFA4A shows homomeric interaction, which is reduced by alanine replacement of three conserved cysteine residues. HSFA4A interacts with mitogen-activated protein kinases MPK3 and MPK6 in yeast and plant cells. MPK3 and MPK6 phosphorylate HSFA4A in vitro on three distinct sites, serine-309 being the major phosphorylation site. Activation of the MPK3 and MPK6 mitogen-activated protein kinase pathway led to the transcriptional activation of the HEAT SHOCK PROTEIN17.6A gene. In agreement that mutation of serine-309 to alanine strongly diminished phosphorylation of HSFA4A, it also strongly reduced the transcriptional activation of HEAT SHOCK PROTEIN17.6A. These data suggest that HSFA4A is a substrate of the MPK3/MPK6 signaling and that it regulates stress responses in Arabidopsis.

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Section: Phosphorylation Of Hsfa4a By Interacting Mpk3 and Mpk6 Kinasesmentioning

confidence: 97%

Section: Phosphorylation Of Hsfa4a By Interacting Mpk3 and Mpk6 Kinasesmentioning

confidence: 99%

The Heat Shock Factor A4A Confers Salt Tolerance and Is Regulated by Oxidative Stress and the Mitogen-Activated Protein Kinases MPK3 and MPK6

et al. 2014

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“…The activation of HAMK in tobacco cells was observed conjunctly with the accumulation of heat shock protein, HSP70, suggesting that HAMK may trigger a heat signaling cascade via HSP genes (Suri and Dhindsa 2008). The activation of HAMK also seems to be calcium dependent in tomato leaves and cells exposed to heat stress (Link et al 2002). Heat and calciumdependent activation of MAP kinases is also observed for MPK6 in Arabidopsis to regulate the activity of vacuolar processing enzyme (VPE) .…”

Section: Mapks and Temperature Stressesmentioning

confidence: 98%

MAPK cascades and major abiotic stresses

et al. 2014

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Plants have evolved with complex signaling circuits that operate under multiple conditions and govern numerous cellular functions. Stress signaling in plant cells is a sophisticated network composed of interacting proteins organized into tiered cascades where the function of a molecule is dependent on the interaction and the activation of another. In a linear scheme, the receptors of cell surface sense the stimuli and convey stress signals through specific pathways and downstream phosphorylation events controlled by mitogen-activated protein (MAP) kinases and second messengers, leading to appropriate adaptive responses. The specificity of the pathway is guided by scaffolding proteins and docking domains inside the interacting partners with distinctive structures and functions. The flexibility and the fine-tuned organization of the signaling molecules drive the activated MAP kinases into the appropriate location and connection to control and integrate the information flow. Here, we overview recent findings of the involvement of MAP kinases in major abiotic stresses (drought, cold and temperature fluctuations) and we shed light on the complexity and the specificity of MAP kinase signaling modules.

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“…In tomato photoautotrophic cell cultures, a partially purified heat activated MAPK was shown to phosphorylate HsFA3 transcription factor. 47 Recently, high and low temperature exhibited an internal rhythm in the activity of MAPK in rice. 48 Another report was published in Solanum tuberosum where heat treatment to potato tubers elevated StMPK1 transcript levels.…”

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confidence: 99%