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Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles
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Summary: Annexins are an homologous, structurally related superfamily of proteins known to associate with membrane lipid and cytoskeletal components. Their involvement in membrane organization, vesicle trafficking and signaling is fundamental to cellular processes such as growth, differentiation, secretion and repair. Annexins exist in some prokaryotes and all eukaryotic phyla within which plant annexins represent a monophyletic clade of homologs descended from green algae. Genomic, proteomic and transcriptomic approaches have provided data on the diversity, cellular localization and expression patterns of different plant annexins. The availability of 35 complete plant genomes has enabled systematic comparative analysis to determine phylogenetic relationships, characterize structures and observe functional specificity between and within individual subfamilies. Short amino termini and selective erosion of the canonical type 2 calcium coordinating sites in domains 2 and 3 are typical of plant annexins. The convergent evolution of alternate functional motifs such as ‘ KGD ’, redox‐sensitive Cys and hydrophobic Trp/Phe residues argues for their functional relevance and contribution to mechanistic diversity in plant annexins. This review examines recent findings and advances in plant annexin research with special focus on their structural diversity, cellular and molecular interactions and their potential integrated functions in the broader context of physiological responses. Contents Summary 695 I. Introduction 695 II. Structural analyses 696 III. Membrane‐related functions 702 IV. Enzyme‐related functions 703 V. Functional insights from proteome and transcriptome analyses 704 VI. Future perspectives 706 Acknowledgements 708 References 708
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“This unusual feature has previously been observed in alpha-giardins and plant annexins (18).”
From Comparative Cell Biology and Evolution of Annexins in Diplomonads (2016) · cites this paper as [18]
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On the pH Regulation of Plant Aquaporins
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Ca 2+ , Annexins, and GTP Modulate Exocytosis from Maize Root Cap Protoplasts
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Regulation of biosynthesis and cellular localization of Sp32 annexins in tobacco BY2 cells
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Annexin V disruption impairs mechanically induced calcium signaling in osteoblastic cells
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GTP-Induced Membrane Binding and Ion Channel Activity of Annexin VI: Is Annexin VI a GTP Biosensor?
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A major cellular substrate for protein kinases, annexin II, is a DNA‐binding protein
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PKCδ‐dependent cleavage and nuclear translocation of annexin A1 by phorbol 12‐myristate 13‐acetate
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A Putative Consensus Sequence for the Nucleotide-Binding Site of Annexin A6
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Annexin 7 mobilizes calcium from endoplasmic reticulum stores in brain
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An Alternative Route for Nuclear mRNP Export by Membrane Budding
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Plant annexins form calcium‐independent oligomers in solution
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Diffusion of Single Cardiac Ryanodine Receptors in Lipid Bilayers Is Decreased by Annexin 12
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Allosterism in Membrane Binding: A Common Motif of the Annexins?
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Mutation of Highly Conserved Arginine Residues Disrupts the Structure and Function of Annexin V
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Metadata
- Authors
- Clark, G. B., Morgan, R. O., Fernandez, M., & Roux, S. J.
- Affiliations
- The University of Texas at Austin (US)
- Universidad de Oviedo (ES)
- Department of Biochemistry and Molecular Biology Faculty of Medicine and University Institute of Biotechnology of Asturias University of Oviedo E‐33006 Oviedo Spain
- Corresponding author
- Roux, Stanley J.
- Venue
- New Phytologist
- Publisher
- Wiley
- Published
- 2012-09-19
- Volume
- 196
- Issue
- 3
- Pages
- 695-712
- ISSN
- 0028-646X (ISSN-L)
- 1469-8137
- OpenAlex
- W2060477111
- Cited by
- 150
- References
- 208
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 8 · 2023: 11 · 2022: 10 · 2021: 27 · 2020: 13 · 2019: 18 · 2018: 10 · 2017: 7 · 2016: 7 · 2015: 13 · 2014: 7 · 2013: 10
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- New Phytologist (publishedVersion)
- PubMed (publishedVersion)
- Consultation of the Doctoral Thesis Database (TESEO) (Ministerio de Educación, Cultura y Deporte) (submittedVersion, cc-by-nc-nd)
- Funders
- Ministerio de Ciencia e Innovación
- National Science Foundation (0718890, 1027514)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- adaptive evolution, phylogenetic relationships, calcium binding sites, membrane organization, vesicle trafficking, cytoskeletal interactions, plant genome
- MeSH terms
- Adaptation, Physiological, Cell Membrane, Markov Chains, Phylogeny, Plant Proteins, Plants, Species Specificity, Structure-Activity Relationship, Genetic Variation, Annexins, Evolution, Molecular, Proteome, Amino Acid Motifs, Gene Expression Profiling, Protein Interaction Mapping
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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