Electrophysiological evidence for a role for calcium in temperature sensing by roots of cucumber seedlings

Minorsky, Peter V.; Spanswick, Roger M.

doi:10.1111/j.1365-3040.1989.tb01925.x

Cited by 65 publications

(70 citation statements)

References 17 publications

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“…Both phases of the voltage transient were reduced by externally applied 1 mM La 3+ , an inhibitor of Ca 2+ -permeable channels (Fig. 4, D-F), which is consistent with the engagement of Ca 2+ -permeable channels at the plasma membrane in cold responses as reported before (Minorsky and Spanswick, 1989;Knight et al, 1996;Lewis and Spalding, 1998;Plieth et al, 1999).…”

Section: +supporting

confidence: 68%

“…Cold shocks elicited voltage transients (also referred to as "signals" here and in the figures) with variable shapes in SEs of control plants, as demonstrated previously (Minorsky and Spanswick, 1989;Thorpe et al, 2010). These transients were often biphasic.…”

Section: +mentioning

confidence: 59%

“…seedlings (Minorsky and Spanswick, 1989). The amplitude of the first transient DV 1 measured in SEs fitted best to the amplitude of the DT in a sigmoid fashion ( Fig.…”

Section: Analysis Of Voltage Transients and Forisome Responses Triggementioning

confidence: 99%

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Involvement of the Sieve Element Cytoskeleton in Electrical Responses to Cold Shocks

Hafke¹,

Ehlers

Föller

et al. 2013

Plant Physiology

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This study dealt with the visualization of the sieve element (SE) cytoskeleton and its involvement in electrical responses to local cold shocks, exemplifying the role of the cytoskeleton in Ca 2+ -triggered signal cascades in SEs. High-affinity fluorescent phalloidin as well as immunocytochemistry using anti-actin antibodies demonstrated a fully developed parietal actin meshwork in SEs. The involvement of the cytoskeleton in electrical responses and forisome conformation changes as indicators of Ca 2+ influx was investigated by the application of cold shocks in the presence of diverse actin disruptors (latrunculin A and cytochalasin D). Under control conditions, cold shocks elicited a graded initial voltage transient, DV 1 , reduced by external La 3+ in keeping with the involvement of Ca 2+ channels, and a second voltage transient, DV 2 . Cytochalasin D had no effect on DV 1 , while DV 1 was significantly reduced with 500 nM latrunculin A. Forisome dispersion was triggered by cold shocks of 4°C or greater, which was indicative of an all-or-none behavior. Forisome dispersion was suppressed by incubation with latrunculin A. In conclusion, the cytoskeleton controls cold shock-induced Ca 2+ influx into SEs, leading to forisome dispersion and sieve plate occlusion in fava bean (Vicia faba).

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Section: +supporting

confidence: 68%

Section: +mentioning

confidence: 59%

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Involvement of the Sieve Element Cytoskeleton in Electrical Responses to Cold Shocks

Hafke¹,

Ehlers

Föller

et al. 2013

Plant Physiology

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“…Low temperature can directly cause microtubule depolymerization. It could also cause microtubule depolymerization indirectly, through such processes as increased cytoplasmic calcium concentration (21). Further work is needed to distinguish between these alternatives.…”

mentioning

confidence: 99%

Relationship between Freezing Tolerance of Root-Tip Cells and Cold Stability of Microtubules in Rye (Secale cereale L. cv Puma)

Kerr¹,

Carter²

1990

Plant Physiol.

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The response of cortical microtubules to low temperature and freezing was assessed for root tips of cold-acclimated and nonacclimated winter rye (Secale cerea/e L. cv Puma) seedlings using indirect immunofluorescence microscopy with antitubulin antibodies. Roots cooled to 0 or -30C were fixed for immunofluorescence microscopy at these temperatures or after an additional hour at 40C. Typical arrays of cortical microtubules were present in root-tip cells of seedlings exposed to the cold-acclimation treatment of 40C for 2 days. Microtubules in these cold-acclimated cells were more easily depolymerized by a 0°C treatment than microtubules in root-tip cells of nonacclimated, 22°C-grown seedlings. Microtubules were still present in some cells of both nonacclimated and cold-acclimated roots at 0 and -30C; however, the number of microtubules in these cells was lower than in controls. Microtubules remaining during the -30C freeze were shorter than microtubules in unfrozen control cells. Repolymenzation of microtubules after both the 0 and -30C treatments occurred within 1 h. Root tips of nonacclimated seedlings had an LT-50 of -90C. Cold acclimation lowered this value to -140C. Treatment of 22°C-grown seedlings for 24 h with the microtubulestabilizing drug taxol caused a decrease in the freezing tolerance of root tips, indicated by a LT-50 of -30C. Treatment with Dsecotaxol, an analog of taxol that was less effective in stabilizing microtubules, did not alter the freezing tolerance. We interpret these data to indicate that a degree of depolymerization of microtubules is necessary for realization of maximum freezing tolerance in root-tip cells of rye.

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“…A transient change in cytosolic calcium levels is one of the initial responses of some plants to adverse environmental conditions such as low temperature, drought, and salinity (16, 19 -23). Several studies show that the ability of plants to withstand calcium level changes is essential for them to survive different abiotic stresses (16,24,25). Typically, cytosolic free calcium is maintained at submicromolecular levels (ϳ200 nM) by homeostatic mechanisms involving a variety of calcium channels, pumps, and secondary transporters in a variety of cell organelles such as vacuole, endoplasmic reticulum, chloroplasts and mitochondria, and cell wall (14,15,26).…”

mentioning

confidence: 99%

Ion Binding Properties of the Dehydrin ERD14 Are Dependent upon Phosphorylation

Alsheikh

Heyen

Randall

2003

Journal of Biological Chemistry

184

194

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The ERD14 protein (early response to dehydration) is a member of the dehydrin family of proteins which accumulate in response to dehydration-related environmental stresses. Here we show the Arabidopsis dehydrin, ERD14, possesses ion binding properties. ERD14 is an in vitro substrate of casein kinase II; the phosphorylation resulting both in a shift in apparent molecular mass on SDS-PAGE gels and increased calcium binding activity. The phosphorylated protein bound significantly more calcium than the nonphosphorylated protein, with a dissociation constant of 120 M and 2.86 mol of calcium bound per mol of protein. ERD14 is phosphorylated by extracts of cold-treated tissues, suggesting that the phosphorylation status of this protein might be modulated by cold-regulated kinases or phosphatases. Calcium binding properties of ERD14 purified from Arabidopsis extracts were comparable with phosphorylated Escherichia coli-expressed ERD14. Approximately 2 mol of phosphate were incorporated per mol of ERD14, indicating a minimum of two phosphorylation sites. Western blot analyses confirmed that threonine and serine are possible phosphorylation sites on ERD14. Utilizing matrix assisted laser desorption ionization-time of flight/ mass spectrometry we identified five phosphorylated peptides that were present in both in vivo and in vitro phosphorylated ERD14. Our results suggest that the polyserine (S) domain is most likely the site of phosphorylation in ERD14 responsible for the activation of calcium binding.

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Electrophysiological evidence for a role for calcium in temperature sensing by roots of cucumber seedlings

Cited by 65 publications

References 17 publications

Involvement of the Sieve Element Cytoskeleton in Electrical Responses to Cold Shocks

Involvement of the Sieve Element Cytoskeleton in Electrical Responses to Cold Shocks

Relationship between Freezing Tolerance of Root-Tip Cells and Cold Stability of Microtubules in Rye (Secale cereale L. cv Puma)

Ion Binding Properties of the Dehydrin ERD14 Are Dependent upon Phosphorylation

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