Cyclic nucleotide-gated cation channel alpha-2 (CNGA2)

Cyclic nucleotide-gated cation channel alpha-2 (CNGA2) is a vital protein in the olfactory signal transduction pathway, primarily localized in the cilia of olfactory sensory neurons [1][2]. It functions as a non-selective cation channel that opens in response to increased intracellular levels of cAMP, which is produced when odorant molecules activate G protein-coupled odorant receptors [3]. The resulting influx of sodium and calcium ions depolarizes the neuron, triggering action potentials that transmit smell information to the brain [1][4]. Beyond its fundamental role in olfaction, CNGA2 is a key model for understanding how cyclic nucleotides regulate ion channel gating and sensory perception [2]. Mutations in the CNGA2 gene are directly linked to anosmia (the loss of the sense of smell), emphasizing its necessity for sensory function [5]. While pharmacological targeting of CNGA2 is currently focused on experimental tools like L-cis-diltiazem, it remains a significant target for research into sensory disorders and potential regenerative therapies for olfactory loss [4][6]. References: [1] UniProt Consortium. (2023). UniProtKB - Q16280 (CNGA2_HUMAN). [2] Pifferi, S., et al. (2006). "The cyclic nucleotide-gated channel of olfactory sensory neurons." Flavour and Fragrance Journal. [3] Kleene, S. J. (2008). "The electrochemical basis of odor transduction." Chemical Senses. [4] Bradley, J., et al. (2005). "The cyclic nucleotide-gated channels of the olfactory system." Chemical Senses. [5] Sailani, M. R., et al. (2017). "Isolated congenital anosmia and CNGA2 mutations." Scientific Reports. [6] Haynes, L. W. (1992). "Block of the cyclic GMP-activated channel of vertebrate rod and cone photoreceptors by l-cis-diltiazem." Visual Neuroscience.

Other names

CNG channel alpha-2Olfactory cyclic nucleotide-gated channel alpha subunitCNCACNCG2CNG2Cyclic nucleotide-gated channel alpha 2

Binding of cyclic nucleotides (cAMP or cGMP) to the intracellular C-terminal domain induces a conformational change that opens the ion-conducting pore, permitting the influx of sodium and calcium ions.