Evidence map›Paper›PMID 22116655›Full record

ArticlePlant molecular biology2012

The Arabidopsis calmodulin-like proteins AtCML30 and AtCML3 are targeted to mitochondria and peroxisomes, respectively.

Fatima Chigri, Sandra Flosdorff, Sahra Pilz, Eva Kölle, Esther Dolze, Christine Gietl, Ute C Vothknecht

Abstract read
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Article in Plant molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 63 citations in OpenAlex.

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  11. Chloroplast Calcium Signaling in the Spotlight.Frontiers in plant science · 2020
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  12. Article
  13. Pharmacological Strategies for Manipulating Plant CaInternational journal of molecular sciences · 2018
    Review
  14. Review
  15. Article
  16. Frontiers in plant science · 2017
    Article
  17. Article
  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 1 country.

Fatima ChigriDepartment of Biology of the LMU Munich, Center for Integrated Protein Science (Munich), 82152 Martinsried, Germany.
Sandra Flosdorff
Sahra Pilz
Eva Kölle
Esther Dolze
Christine Gietl
Ute C Vothknecht
Ludwig-Maximilians-Universität München · DEMax Planck Institute of Neurobiology · DECenter for Integrated Protein Science Munich · DETechnical University of Munich · DEWeihenstephan-Triesdorf University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calmodulin (CaM) is a ubiquitous sensor/transducer of calcium signals in eukaryotic organisms. While CaM mediated calcium regulation of cytosolic processes is well established, there is growing evidence for the inclusion of organelles such as chloroplasts, mitochondria and peroxisomes into the calcium/calmodulin regulation network. A number of CaM-binding proteins have been identified in these organelles and processes such as protein import into chloroplasts and mitochondria have been shown to be governed by CaM regulation. What have been missing to date are the mediators of this regulation since no CaM or calmodulin-like protein (CML) has been identified in any of these organelles. Here we show that two Arabidopsis CMLs, AtCML3 and AtCML30, are localized in peroxisomes and mitochondria, respectively. AtCML3 is targeted via an unusual C-terminal PTS1-like tripeptide while AtCML30 utilizes an N-terminal, non-cleavable transit peptide. Both proteins possess the typical structure of CaMs, with two pairs of EF-hand motifs separated by a short linker domain. They furthermore display common characteristics, such as calcium-dependent alteration of gel mobility and calcium-dependent exposure of a hydrophobic surface. This indicates that they can function in a similar manner as canonical CaMs. The presence of close homologues to AtCML3 and AtCML30 in other plants further indicates that organellar targeting of these CMLs is not a specific feature of Arabidopsis. The identification of peroxisomal and mitochondrial CMLs is an important step in the understanding how these organelles are integrated into the cellular calcium/calmodulin signaling pathways.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBacterial ProteinsBiological Transport, ActiveCalmodulinIntracellular Calcium-Sensing ProteinsLuminescent ProteinsMitochondriaMolecular Sequence DataNicotianaPeroxisomesPhylogenyPlants, Genetically ModifiedProtein ConformationRecombinant Fusion ProteinsArabidopsis ProteinsBacterial ProteinsCalmodulinCML3 protein, ArabidopsisIntracellular Calcium-Sensing ProteinsLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID22116655
OpenAlexW2027728593

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.