ArticlePlant physiology1994
A 42-kilodalton annexin-like protein is associated with plant vacuoles.
Article in Plant physiology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Genome-Wide Characterization and Abiotic Stresses Expression Analysis of Annexin Family Genes in Poplar.International journal of molecular sciences · 2022Article
- Transport, functions, and interaction of calcium and manganese in plant organellar compartments.Plant physiology · 2021Review
- Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells.International journal of molecular sciences · 2017Review
- Identification and characterization of annexin gene family in rice.Plant cell reports · 2012Article
- Annexins: putative linkers in dynamic membrane-cytoskeleton interactions in plant cells.Protoplasma · 2007Review
- The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation.Plant physiology · 2002Article
- Plant annexins form calcium-independent oligomers in solution.Protein science : a publication of the Protein Society · 2002Article
- Dynamic localization of rop GTPases to the tonoplast during vacuole development.Plant physiology · 2001Article
- GTPase activity and biochemical characterization of a recombinant cotton fiber annexin.Plant physiology · 1999Article
- Tomato annexins p34 and p35 bind to F-actin and display nucleotide phosphodiesterase activity inhibited by phospholipid binding.The Plant cell · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 42-kD, calcium-dependent, membrane-binding protein (VCaB42) was associated with partially purified vacuole membrane. Membrane-dissociation assays indicated that VCaB42 binding to vacuole membranes was selective for calcium over other cations and that 50% of VCaB42 remained membrane bound at 61 +/- 11 nM free calcium. A 13-amino acid sequence obtained from VCaB42 showed 85% similarity with the endonexin fold, a sequence found in the annexin family of proteins that is thought to be essential for calcium and lipid binding. The greatest similarity in amino acid sequence was observed with annexin VIII (VAC-beta). The calcium-binding properties and sequence similarities suggest that VCaB42 is a member of the annexin family of calcium-dependent, membrane-binding proteins. Functional assays for VCaB42 on vacuole membrane transport processes indicated that it did not significantly affect the initial rate of calcium uptake into vacuole membrane vesicles. Because VCaB42 is vacuole localized (likely on the cytosolic surface of the vacuole) and is 50% dissociated within the physiological range of cytosolic free calcium, we hypothesize that this protein is a sensor that monitors cytosolic calcium levels and transmits that information to the vacuole.
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Registered trials
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