ArticlePlant physiology2000
At-ACA8 encodes a plasma membrane-localized calcium-ATPase of Arabidopsis with a calmodulin-binding domain at the N terminus.
Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 124 citations in OpenAlex.
- Aspects of plant intelligence (ii).Plant signaling & behavior · 2026Review
- Understanding the role of P-type ATPases in regulating pollen fertility and development in pigeonpea.Molecular genetics and genomics : MGG · 2024Article
- Resting cytosol Ca2+ level maintained by Ca2+ pumps affects environmental responses in Arabidopsis.Plant physiology · 2023Article
- Structural Analysis and Diversity of Calmodulin-Binding Domains in Membrane and Intracellular CaThe Journal of membrane biology · 2023Article
- Genetic Analyses of Seed Longevity inPlants (Basel, Switzerland) · 2023Article
- Transcriptomic analysis unravels the molecular response ofFrontiers in plant science · 2022Article
- Calcium channels and transporters: Roles in response to biotic and abiotic stresses.Frontiers in plant science · 2022Review
- Evolutionary and Regulatory Pattern Analysis of Soybean CaFrontiers in plant science · 2022Article
- When everything changes at once: finding a new normal after genome duplication.Proceedings. Biological sciences · 2020Article
- Fertilization in flowering plants: an odyssey of sperm cell delivery.Plant molecular biology · 2020Review
- Plasma Membrane-Localized Calcium Pumps and Copines Coordinately Regulate Pollen Germination and Fertility in Arabidopsis.International journal of molecular sciences · 2018Article
- Overlapping and differential roles of plasma membrane calcium ATPases in Arabidopsis growth and environmental responses.Journal of experimental botany · 2018Article
- Calcium Signalling in Plant Biotic Interactions.International journal of molecular sciences · 2018Review
- Structural basis for activation of plasma-membrane CaCommunications biology · 2018Article
- Article
- Calcium Pumps and Interacting BON1 Protein Modulate Calcium Signature, Stomatal Closure, and Plant Immunity.Plant physiology · 2017Article
- The Membrane Transport System of the Guard Cell and Its Integration for Stomatal Dynamics.Plant physiology · 2017Review
- Ca2+-dependent phosphoregulation of the plasma membrane Ca2+-ATPase ACA8 modulates stimulus-induced calcium signatures.Journal of experimental botany · 2017Article
- Genome-wide expression profiling in leaves and roots of date palm (Phoenix dactylifera L.) exposed to salinity.BMC genomics · 2017Article
- Identification of Candidate Genes for Calcium and Magnesium Accumulation inFrontiers in plant science · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A Ca(2+)-ATPase was purified from plasma membranes (PM) isolated from Arabidopsis cultured cells by calmodulin (CaM)-affinity chromatography. Three tryptic fragments from the protein were microsequenced and the corresponding cDNA was amplified by polymerase chain reaction using primers designed from the microsequences of the tryptic fragments. At-ACA8 (Arabidopsis-autoinhibited Ca(2+)-ATPase, isoform 8, accession no. AJ249352) encodes a 1,074 amino acid protein with 10 putative transmembrane domains, which contains all of the characteristic motifs of Ca(2+)-transporting P-type Ca(2+)-ATPases. The identity of At-ACA8p as the PM Ca(2+)-ATPase was confirmed by immunodetection with an antiserum raised against a sequence (valine-17 through threonine-31) that is not found in other plant CaM-stimulated Ca(2+)-ATPases. Confocal fluorescence microscopy of protoplasts immunodecorated with the same antiserum confirmed the PM localization of At-ACA8. At-ACA8 is the first plant PM localized Ca(2+)-ATPase to be cloned and is clearly distinct from animal PM Ca(2+)-ATPases due to the localization of its CaM-binding domain. CaM overlay assays localized the CaM-binding domain of At-ACA8p to a region of the N terminus of the enzyme around tryptophan-47, in contrast to a C-terminal localization for its animal counterparts. Comparison between the sequence of At-ACA8p and those of endomembrane-localized type IIB Ca(2+)-ATPases of plants suggests that At-ACA8 is a representative of a new subfamily of plant type IIB Ca(2+)-ATPases.
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