The Calcium Sensor Protein Visinin-like Protein-1 Modulates the Surface Expression and Agonist Sensitivity of the α4β2 Nicotinic Acetylcholine Receptor*
By Lin-Li Lin, E. Jeanclos, Magdalen W. Treuil, K. Braunewell, E. Gundelfinger, R. Anand. Journal of Biological Chemistry, 2002
106 citations recorded by the source corpus.
The calcium sensor protein visinin-like protein-1 (VILIP-1) was isolated from a brain cDNA yeast two-hybrid library using the large cytoplasmic domain of the α4 subunit as a bait. VILIP-1 is a myristoylated calcium sensor protein that contains three functional calcium binding EF-hand motifs. The α4 subunit residues 302–339 were found to be essential for the interaction with VILIP-1. VILIP-1 coimmunopurified with detergent-solubilized recombinant α4β2 acetylcholine receptors (AChRs) expressed in tsA201 cells and with native α4 AChRs isolated from brain. Coexpression of VILIP-1 with recombinant α4β2 AChRs up-regulated their surface expression levels ∼2-fold and increased their agonist sensitivity to acetylcholine ∼3-fold. The modulation of the recombinant α4β2 AChRs by VILIP-1 was attenuated in VILIP-1 mutants that lacked the ability to be myristoylated or to bind calcium. Collectively, these results suggest that VILIP-1 represents a novel modulator of α4β2 AChRs that increases their surface expression levels and agonist sensitivity in response to changes in the intracellular levels of calcium.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/d39e41d2c6bedf87f9c8eeb4d0cef6914fbd5b2f
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In Cellular and Molecular Neuroscience
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Citations in the corpus
- Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system (2009, background): “The cytoplasmic domain of the α4 nAChR subunit binds the scaffold protein 14-3-3η and the Ca 2+ sensor visinin-like protein 1 (Ref”