ArticleThe EMBO journal1999
The prenylation status of a novel plant calmodulin directs plasma membrane or nuclear localization of the protein.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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.
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.
Who cites it
60 citing papers in PubMed, 159 citations in OpenAlex.
- Article
- CML20 integrates phytochrome and calcium signaling pathways to optimize seed germination under abiotic stress.Nature communications · 2026Article
- Farnesol and geranylgeraniol in plant reproduction: insights from Arabidopsis and beyond.Journal of experimental botany · 2026Review
- Protein Prenylation Makeovers in Plants: Insights into Substrate Diversification.International journal of molecular sciences · 2025Review
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Methyl-Jasmonate Functions as a Molecular Switch Promoting Cross-Talk between Pathways for the Biosynthesis of Isoprenoid Backbones Used to Modify Proteins in Plants.Plants (Basel, Switzerland) · 2024Article
- The Re-Localization of Proteins to or Away from Membranes as an Effective Strategy for Regulating Stress Tolerance in Plants.Membranes · 2022Review
- Calmodulin7: recent insights into emerging roles in plant development and stress.Plant molecular biology · 2021Review
- Review
- Calmodulin is involved in the dual subcellular location of two chloroplast proteins.The Journal of biological chemistry · 2019Article
- Protein Prenylation in Plant Stress Responses.Molecules (Basel, Switzerland) · 2019Review
- Calmodulin Is the Fundamental Regulator of NADK-Mediated NAD Signaling in Plants.Frontiers in plant science · 2019Article
- Overexpression ofFrontiers in plant science · 2018Article
- Corrected and Republished from: Activation Status-Coupled Transient S-Acylation Determines Membrane Partitioning of a Plant Rho-Related GTPase.Molecular and cellular biology · 2017Article
- Genome-Wide Identification and Analyses of Calmodulins and Calmodulin-like Proteins inFrontiers in plant science · 2017Article
- Abiotic stress responses in plants: roles of calmodulin-regulated proteins.Frontiers in plant science · 2015Review
- Development of an image-based screening system for inhibitors of the plastidial MEP pathway and of protein geranylgeranylation.F1000Research · 2015Article
- Structural analysis of a calmodulin variant from rice: the C-terminal extension of OsCaM61 regulates its calcium binding and enzyme activation properties.The Journal of biological chemistry · 2013Article
- Nuclear calcium signaling in plants.Plant physiology · 2013Review
- Leveraging proteomics to understand plant-microbe interactions.Frontiers in plant science · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational attachment of isoprenyl groups to conserved cysteine residues at the C-terminus of a number of regulatory proteins is important for their function and subcellular localization. We have identified a novel calmodulin, CaM53, with an extended C-terminal basic domain and a CTIL CaaX-box motif which are required for efficient prenylation of the protein in vitro and in vivo. Ectopic expression of wild-type CaM53 or a non-prenylated mutant protein in plants causes distinct morphological changes. Prenylated CaM53 associates with the plasma membrane, but the non-prenylated mutant protein localizes to the nucleus, indicating a dual role for the C-terminal domain. The subcellular localization of CaM53 can be altered by a block in isoprenoid biosynthesis or sugar depletion, suggesting that CaM53 activates different targets in response to metabolic changes. Thus, prenylation of CaM53 appears to be a novel mechanism by which plant cells can coordinate Ca2+ signaling with changes in metabolic activities.
Indexed as
Identifiers
What OpenQuestion holds
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.