ArticlePlant molecular biology2002
The subcellular localization of an unusual rice calmodulin isoform, OsCaM61, depends on its prenylation status.
Article in Plant molecular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 36 citations in OpenAlex.
- A rice calmodulin-like protein OsCML27 participates in drought tolerance by fine-tuning OsRbohB-mediated ROS signaling.Science advances · 2026Article
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Calmodulin Is the Fundamental Regulator of NADK-Mediated NAD Signaling in Plants.Frontiers in plant science · 2019Article
- 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
- Article
- The plastidial 2-C-methyl-D-erythritol 4-phosphate pathway provides the isoprenyl moiety for protein geranylgeranylation in tobacco BY-2 cells.The Plant cell · 2009Article
- Genome-wide identification and analyses of the rice calmodulin and related potential calcium sensor proteins.BMC plant biology · 2007Article
- Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals.Plant signaling & behavior · 2006Article
- Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants.Plant physiology · 2005Article
- Farnesylated peptides in model membranes: a biophysical investigation.European biophysics journal : EBJ · 2004Article
- Calcium in plants.Annals of botany · 2003Review
- Calmodulins and calcineurin B-like proteins: calcium sensors for specific signal response coupling in plants.The Plant cell · 2002Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin (CaM) is a small Ca2+-binding protein highly conserved in eukaryotes. We have reported previously a novel rice CaM-like protein (OsCaM61) which contains an N-terminal CaM domain and a C-terminal extension with a potential prenylation site. Here we report in vitro activity assays confirm OsCaM61 as a functional CaM. Using the green fluorescent protein (GFP) as a visual marker, we further studied the subcellular localization of OsCaM61 in stably transformed tobacco cells. The GFP-OsCaM61 fusion protein was membrane-associated whereas OsCaM61-GFP was mainly detected in the nucleoplasm. GFP-OsCaM61 was transported into the nucleoplasm upon a block in isoprenoid biosynthesis by mevinolin treatment of cells. These results indicate that the prenylated OsCaM61 molecules are mainly membrane-associated whereas its unprenylated counterparts are transported into the nucleoplasm. Thus, OsCaM61 may play functions in co-ordinating Ca2+ signaling with isoprenoid metabolism.
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