ArticlePloS one2011
Determination of the membrane topology of the small EF-hand Ca2+-sensing proteins CaBP7 and CaBP8.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Structure-Function Diversity of Calcium-Binding Proteins (CaBPs): Key Roles in Cell Signalling and Disease.Cells · 2025Review
- Calcium-Associated Proteins in Neuroregeneration.Biomolecules · 2024Review
- Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019Review
- Caldendrin and Calneurons-EF-Hand CaM-Like Calcium Sensors With Unique Features and Specialized Neuronal Functions.Frontiers in molecular neuroscience · 2019Review
- Alternative splicing, expression and cellular localization of Calneuron-1 in the rat and human brain.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015Article
- Sense and specificity in neuronal calcium signalling.Biochimica et biophysica acta · 2015Review
- Modulation of phosphatidylinositol 4-phosphate levels by CaBP7 controls cytokinesis in mammalian cells.Molecular biology of the cell · 2015Article
- Generation and characterization of a lysosomally targeted, genetically encoded Ca(2+)-sensor.The Biochemical journal · 2013Article
- Solution NMR structure of the Ca2+-bound N-terminal domain of CaBP7: a regulator of golgi trafficking.The Journal of biological chemistry · 2012Article
- Evolution and functional diversity of the Calcium Binding Proteins (CaBPs).Frontiers in molecular neuroscience · 2012Article
- Ca(2+) sensor proteins in dendritic spines: a race for Ca(2+).Frontiers in molecular neuroscience · 2012Article
- Post-translational membrane insertion of tail-anchored transmembrane EF-hand Ca2+ sensor calneurons requires the TRC40/Asna1 protein chaperone.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The CaBPs represent a subfamily of small EF-hand containing calcium (Ca(2+))-sensing proteins related to calmodulin that regulate key ion channels in the mammalian nervous system. In a recent bioinformatic analyses we determined that CaBP7 and CaBP8 form an evolutionarily distinct branch within the CaBPs (also known as the calneurons) a finding that is consistent with earlier observations characterising a putative C-terminal transmembrane (TM) spanning helix in each of these proteins which is essential for their sub-cellular targeting to the Golgi apparatus and constitutive secretory vesicles. The C-terminal position of the predicted TM-helix suggests that CaBP7 and CaBP8 could be processed in a manner analogous to tail-anchored integral membrane proteins which exhibit the ability to insert across membranes post-translationally. In this study we have investigated the topology of CaBP7 and CaBP8 within cellular membranes through a combination of trypsin protection and epitope accessibility analyses. Our results indicate that the TM-helices of CaBP7 and CaBP8 insert fully across membranes such that their extreme C-termini are luminal. The observed type-II membrane topology is consistent with processing of CaBP7 and CaBP8 as true tail-anchored proteins. This targeting mechanism is distinct from any other calmodulin related Ca(2+)-sensor and conceivably underpins unique physiological functions of these proteins.
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