The outer membrane of plant mitochondria contains a calcium‐dependent protein kinase and multiple phosphoproteins

Pical, Christophe; Fredlund, Kenneth M.; Petit, Patrice X.; Sommarin, Marianne; Møller, lan M.

doi:10.1016/0014-5793(93)80835-i

Cited by 49 publications

(40 citation statements)

References 33 publications

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“…Previously, a recessive mutation in the porin gene has been shown to cause lethality or elevated early mortality and to be expressed in a sex-specific pattern (Oliva et al, 2002;Lee et al, 2007). Sixteen potential phosphorylation sites have been identified on the D. melanogaster porin protein, indicating a very fine-tuned regulation by posttranslational phosphorylation (Pical et al, 1993;Lee et al, 2007). This may imply increased mutational constrains, and as a result optimal function of porin may be highly vulnerable.…”

Section: Mitochondrial-related Processesmentioning

confidence: 99%

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

et al. 2009

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Genetic variation that is expressed only under specific environmental conditions can contribute to additional adverse effects of inbreeding if environmental conditions change. We present a proteomic characterization of a conditional lethal found in an inbred line of Drosophila melanogaster. The lethal effect is apparent as a large increase in early mortality at the restrictive temperature (29 1C) as opposed to normal survival at the permissive temperature (20 1C). The increased mortality in response to the restrictive temperature is probably caused by a single recessive major locus. A quantitative trait locus (QTL) region segregating variation affecting the lethal effect has been identified, allowing for a separation of primary/causal effects and secondary consequences in the proteome expression patterns observed. In this study, the proteomic response to the restrictive temperature in the lethal-line (L-line) was compared with the response in an inbred-control-line (IC-line) and an outbred-control-line (OC-line). Quantitative protein changes were detected using isobaric tags for relative and absolute quantitation (iTRAQ) two-dimensional liquid chromatography-tandem mass spectrometry. In all, 45 proteins were found to be significantly differently regulated in response to the restrictive temperature in the L-line as compared with the IC-line. No proteins were significantly differently regulated between the IC-line and the OC-line, verifying that differential protein regulation was specific to a genetic defect in the L-line. Proteins associated with oxidative phosphorylation and mitochondria were significantly overrepresented within the list of differentially expressed proteins. Proteins related to muscle contraction were also found to be differentially expressed in the L-line in response to the restrictive temperature, supporting phenotypic observations of moribund muscle hypercontraction.

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Section: Mitochondrial-related Processesmentioning

confidence: 99%

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

et al. 2009

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“…CDPK isoforms localize to a variety of intracellular locations, including the cytosol, nucleus, plasma membrane, endoplasmic reticulum, peroxisomes, mitochondrial outer membrane, and oil bodies (Pical et al, 1993;Patharkar and Cushman, 2000;Lu and Hrabak, 2002;Anil et al, 2003;Dammann et al, 2003). We employed confocal microscopy to assess the subcellular localization of each CDPK isoform using full-length C-terminal GFP fusions.…”

Section: Localization Of Pi Cdpk1 and Pi Cdpk2mentioning

confidence: 99%

Calcium-Dependent Protein Kinase Isoforms inPetuniaHave Distinct Functions in Pollen Tube Growth, Including Regulating Polarity

et al. 2006

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Calcium is a key regulator of pollen tube growth, but little is known concerning the downstream components of the signaling pathways involved. We identified two pollen-expressed calmodulin-like domain protein kinases from Petunia inflata, CALMODULIN-LIKE DOMAIN PROTEIN KINASE1 (Pi CDPK1) and Pi CDPK2. Transient overexpression or expression of catalytically modified Pi CDPK1 disrupted pollen tube growth polarity, whereas expression of Pi CDPK2 constructs inhibited tube growth but not polarity. Pi CDPK1 exhibited plasma membrane localization most likely mediated by acylation, and we present evidence that suggests this localization is critical to the biological function of this kinase. Pi CDPK2 substantially localized to as yet unidentified internal membrane compartments, and this localization was again, at least partially, mediated by acylation. In contrast with Pi CDPK1, altering the localization of Pi CDPK2 did not noticeably alter the effect of overexpressing this isoform on pollen tube growth. Ca2+ requirements for Pi CDPK1 activation correlated closely with Ca2+ concentrations measured in the growth zone at the pollen tube apex. Interestingly, loss of polarity associated with overexpression of Pi CDPK1 was associated with elevated cytosolic Ca2+ throughout the bulging tube tip, suggesting that Pi CDPK1 may participate in maintaining Ca2+ homeostasis. These results are discussed in relation to previous models for Ca2+ regulation of pollen tube growth.

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“…In yeast, cAMP-dependent protein kinase activity has been observed in association with inner mitochondrial membranes [4]. In plant mitochondria, more than 20 substrates for protein phosphorylation have been detected [7,12,13].…”

Section: Introductionmentioning

confidence: 99%

Histidine and tyrosine phosphorylation in pea mitochondria: evidence for protein phosphorylation in respiratory redox signalling

Håk̈ansson

Allen

1995

FEBS Letters

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A 37 kDa protein in pea mitochondria was found to contain phosphorylated residues. Phosphorylation was acid-labile but stable in alkali solution, a unique property of phosphorylation on histidine, indicating that a signal transduction pathway with homology to bacterial two-component systems might exist in plant mitochondria. We also describe the first example of tyrosine phosphorylation in plant organelles and the first indication of protein phosphorylation as part of a redox signalling mechanism in mitochondria. Labelling of three proteins (28, 27 and 12 kDa) was found to be dependent on the redox state of the reaction medium. Their phospho-groups were resistant to alkali as well as acid treatment and labelling was inhibited by the tyrosine kinase inhibitor genistein.

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The outer membrane of plant mitochondria contains a calcium‐dependent protein kinase and multiple phosphoproteins

Cited by 49 publications

References 33 publications

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

Proteomic characterization of a temperature-sensitive conditional lethal in Drosophila melanogaster

Calcium-Dependent Protein Kinase Isoforms inPetuniaHave Distinct Functions in Pollen Tube Growth, Including Regulating Polarity

Histidine and tyrosine phosphorylation in pea mitochondria: evidence for protein phosphorylation in respiratory redox signalling

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