ArticlePlant physiology2003
Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants.
Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 83 citations in OpenAlex.
- Plant-specific calreticulin is localized in the nuclei of highly specialized cells in the pistil-new observations for an old hypothesis.Protoplasma · 2024Article
- Comprehensive genomic characterization and expression analysis of calreticulin gene family in tomato.Frontiers in plant science · 2024Article
- Endoplasmic reticulum calnexins participate in the primary root growth response to phosphate deficiency.Plant physiology · 2023Article
- Growing Maize Root: Lectins Involved in Consecutive Stages of Cell Development.Plants (Basel, Switzerland) · 2022Article
- RNAi-Mediated Knockdown of Calreticulin3a Impairs Pollen Tube Growth inInternational journal of molecular sciences · 2022Article
- Calreticulin expression and localization in relation to exchangeable CaBMC plant biology · 2022Article
- Identification of Phytaspase Interactors via the Proximity-Dependent Biotin-Based Identification Approach.International journal of molecular sciences · 2021Article
- Mechanism of Salt-Induced Self-Compatibility Dissected by Comparative Proteomic Analysis inInternational journal of molecular sciences · 2018Article
- Protein Quality Control in the Endoplasmic Reticulum of Plants.Annual review of plant biology · 2018Review
- Characterisation of Arabidopsis calnexin 1 and calnexin 2 in the endoplasmic reticulum and at plasmodesmata.Protoplasma · 2017Article
- Functional Analysis and Marker Development ofFrontiers in plant science · 2017Article
- Isolation and Characterization of Pepper Genes Interacting with the CMV-P1 Helicase Domain.PloS one · 2016Article
- Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- EBS7 is a plant-specific component of a highly conserved endoplasmic reticulum-associated degradation system in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Molecular characterisation and expression analysis of a novel calreticulin (CRT) gene in the dinoflagellate Prorocentrum minimum.Molecular biology reports · 2015Article
- Proteomics, metabolomics, and ionomics perspectives of salinity tolerance in halophytes.Frontiers in plant science · 2015Review
- Overexpression of a Triticum aestivum Calreticulin gene (TaCRT1) Improves Salinity Tolerance in Tobacco.PloS one · 2015Article
- Article
- Proteomic analysis of salt-responsive proteins in the leaves of mangrove Kandelia candel during short-term stress.PloS one · 2014Article
- The ER quality control and ER associated degradation machineries are vital for viral pathogenesis.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calreticulin (CRT) is a multifunctional protein mainly localized to the endoplasmic reticulum in eukaryotic cells. Here, we present the first analysis, to our knowledge, of evolutionary diversity and expression profiling among different plant CRT isoforms. Phylogenetic studies and expression analysis show that higher plants contain two distinct groups of CRTs: a CRT1/CRT2 group and a CRT3 group. To corroborate the existence of these isoform groups, we cloned a putative CRT3 ortholog from Brassica rapa. The CRT3 gene appears to be most closely related to the ancestral CRT gene in higher plants. Distinct tissue-dependent expression patterns and stress-related regulation were observed for the isoform groups. Furthermore, analysis of posttranslational modifications revealed differences in the glycosylation status among members within the CRT1/CRT2 isoform group. Based on evolutionary relationship, a new nomenclature for plant CRTs is suggested. The presence of two distinct CRT isoform groups, with distinct expression patterns and posttranslational modifications, supports functional specificity among plant CRTs and could account for the multiple functional roles assigned to CRTs.
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