ArticleThe Journal of biological chemistry2019
Calmodulin is involved in the dual subcellular location of two chloroplast proteins.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- The fluorescence-activating and absorption-shifting tag (FAST), a versatile protein marker for live plant cell imaging.The Plant journal : for cell and molecular biology · 2026Article
- CaBMC plant biology · 2025Article
- Integration analysis of ATAC-seq and RNA-seq provides insight into fatty acid biosynthesis in Schizochytrium limacinum under nitrogen limitation stress.BMC genomics · 2024Article
- Isolation of Cytosolic Ribosomes Associated with Plant Mitochondria and Chloroplasts.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Establishment of a Landscape of UPL5-Ubiquitinated on Multiple Subcellular Components of Leaf Senescence Cell inInternational journal of molecular sciences · 2022Article
- Evidence Supporting an Antimicrobial Origin of Targeting Peptides to Endosymbiotic Organelles.Cells · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
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Abstract
Cell compartmentalization is an essential process by which eukaryotic cells separate and control biological processes. Although calmodulins are well-known to regulate catalytic properties of their targets, we show here their involvement in the subcellular location of two plant proteins. Both proteins exhibit a dual location, namely in the cytosol in addition to their association to plastids (where they are known to fulfil their role). One of these proteins, ceQORH, a long-chain fatty acid reductase, was analyzed in more detail, and its calmodulin-binding site was identified by specific mutations. Such a mutated form is predominantly targeted to plastids at the expense of its cytosolic location. The second protein, TIC32, was also shown to be dependent on its calmodulin-binding site for retention in the cytosol. Complementary approaches (bimolecular fluorescence complementation and reverse genetics) demonstrated that the calmodulin isoform CAM5 is specifically involved in the retention of ceQORH in the cytosol. This study identifies a new role for calmodulin and sheds new light on the intriguing CaM-binding properties of hundreds of plastid proteins, despite the fact that no CaM or CaM-like proteins were identified in plastids.
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Registered trials
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.