| Reference code: | PT/FB/BL-2004-009.02 |
| Location: | Arquivo PCA - Pasta 8/2004
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Title:
| Divalent cations and redox conditions regulate the molecular structure and function of Visinin-like Protein 1
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| Publication year: | 2011
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URL:
| http://www.plosone.org/article/fetchObject.action?uri=info%3Adoi%2F10.1371%2Fjournal.pone.0026793&representation=PDF
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| Abstract/Results: | ABSTRACT:
The NCS protein Visinin-like Protein 1 (VILIP-1) transduces calcium signals in the brain and serves as an effector of the non-retinal receptor guanylyl cyclases (GCs) GC-A and GC-B, and nicotinic acetyl choline receptors (nAchR). Analysis of the quaternary structure of VILIP-1 in solution reveals the existence of monomeric and dimeric species, the relative contents of which are affected but not exclusively regulated by divalent metal ions and Redox conditions. Using small-angle X-ray scattering, we have investigated the low resolution structure of the calcium-bound VILIP-1 dimer under reducing conditions. Scattering profiles for samples with high monomeric and dimeric contents have been obtained. The dimerization interface involves residues from EF-hand regions EF3 and EF4.Using monolayer adsorption experiments, we show that myristoylated and unmyristoylated VILIP-1 can bind lipid membranes. The presence of calcium only marginally improves binding of the protein to the monolayer, suggesting that charged residues at the protein surface may play a role in the binding process.In the presence of calcium, VILIP-1 undergoes a conformational re-arrangement, exposing previously hidden surfaces for interaction with protein partners. We hypothesise a working model where dimeric VILIP-1 interacts with the membrane where it binds membrane-bound receptors in a calcium-dependent manner.
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| Accessibility: | Document does not exist in file
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Language:
| eng
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Author:
| Wang, C. K.
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Secondary author(s):
| Simon, A., Jessen, C. M., Oliveira, C. L., Mack, L., Braunewell, K.-H., Ames, J. B., Pedersen, J. S., Hofmann, A.
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Document type:
| Article
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Number of reproductions:
| 1
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Reference:
| Wang, C. K., Simon, A., Jessen, C. M., Oliveira, C. L., Mack, L., Braunewell, K.-H., . . . Hofmann, A. (2011). Divalent cations and redox conditions regulate the molecular structure and function of Visinin-like Protein 1. PLoS ONE, 6(11), e26793. https://doi.org/10.1371/journal.pone.0026793
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| 2-year Impact Factor: | 4.092|2011
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| Times cited: | 12|2024-02-01
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| Indexed document: | Yes
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| Quartile: | Q1
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| Keywords: | Psychophysiology / Guanylyl cyclase / Neuronal calcium sensors / Visinin-like proteins
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Divalent cations and redox conditions regulate the molecular structure and function of Visinin-like Protein 1 |