ArticleThe Biochemical journal2000
Differential regulation of Ca2+/calmodulin-dependent enzymes by plant calmodulin isoforms and free Ca2+ concentration.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 85 citations in OpenAlex.
- Delineating Calcium Signaling Machinery in Plants: Tapping the Potential through Functional Genomics.Current genomics · 2021Review
- Cross Talk Between Cyclic Nucleotides and Calcium Signaling Pathways in Plants-Achievements and Prospects.Frontiers in plant science · 2021Review
- Molecular Players of EF-hand Containing Calcium Signaling Event in Plants.International journal of molecular sciences · 2019Review
- Metal Ion Modeling Using Classical Mechanics.Chemical reviews · 2017Review
- Regulation of Pulmonary Vascular Smooth Muscle Contractility in Pulmonary Arterial Hypertension: Implications for Therapy.Frontiers in physiology · 2017Review
- Divergent Soybean Calmodulins Respond Similarly to Calcium Transients: Insight into Differential Target Regulation.Frontiers in plant science · 2017Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- Involvement of calmodulin and calmodulin-like proteins in plant responses to abiotic stresses.Frontiers in plant science · 2015Review
- Functions of Calcium-Dependent Protein Kinases in Plant Innate Immunity.Plants (Basel, Switzerland) · 2014Review
- Comparing the calcium binding abilities of two soybean calmodulins: towards understanding the divergent nature of plant calmodulins.The Plant cell · 2013Article
- 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
- The solution structure of a plant calmodulin and the CaM-binding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism.The Journal of biological chemistry · 2010Article
- AtCML8, a calmodulin-like protein, differentially activating CaM-dependent enzymes in Arabidopsis thaliana.Plant cell reports · 2010Article
- The solution structure of the Mg2+ form of soybean calmodulin isoform 4 reveals unique features of plant calmodulins in resting cells.Protein science : a publication of the Protein Society · 2010Article
- Structural studies of soybean calmodulin isoform 4 bound to the calmodulin-binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode.The Journal of biological chemistry · 2009Article
- Plant calmodulins and calmodulin-related proteins: multifaceted relays to decode calcium signals.Plant signaling & behavior · 2006Article
- Pathogen- and NaCl-induced expression of the SCaM-4 promoter is mediated in part by a GT-1 box that interacts with a GT-1-like transcription factor.Plant physiology · 2004Article
- Characterization of a novel calcium/calmodulin-dependent protein kinase from tobacco.Plant physiology · 2004Article
- Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides.Molecular biotechnology · 2004Review
- KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a microtubule motor protein and regulates trichome morphogenesis.The Plant cell · 2004Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Multiple calmodulin (CaM) isoforms are expressed in plants, but their biochemical characteristics are not well resolved. Here we show the differential regulation exhibited by two soya bean CaM isoforms (SCaM-1 and SCaM-4) for the activation of five CaM-dependent enzymes, and the Ca(2+) dependence of their target enzyme activation. SCaM-1 activated myosin light-chain kinase as effectively as brain CaM (K(act) 1.8 and 1.7 nM respectively), but SCaM-4 produced no activation of this enzyme. Both CaM isoforms supported near maximal activation of CaM-dependent protein kinase II (CaM KII), but SCaM-4 exhibited approx.12-fold higher K(act) than SCaM-1 for CaM KII phosphorylation of caldesmon. The SCaM isoforms showed differential activation of plant and animal Ca(2+)-ATPases. The plant Ca(2+)-ATPase was activated maximally by both isoforms, while the erythrocyte Ca(2+)-ATPase was activated only by SCaM-1. Plant glutamate decarboxylase was activated fully by SCaM-1, but SCaM-4 exhibited an approx. 4-fold increase in K(act) and an approx. 25% reduction in V(max). Importantly, SCaM isoforms showed a distinct Ca(2+) concentration requirement for target enzyme activation. SCaM-4 required 4-fold higher [Ca(2+)] for half-maximal activation of CaM KII, and 1.5-fold higher [Ca(2+)] for activation of cyclic nucleotide phosphodiesterase than SCaM-1. Thus these plant CaM isoforms provide a mechanism by which a different subset of target enzymes could be activated or inhibited by the differential expression of these CaM isoforms or by differences in Ca(2+) transients.
Indexed as
Identifiers
10926857PMC1221255W2070617335What 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.