glycine-gated chloride ion channel activity

Definition

Target type: molecularfunction

Enables the transmembrane transfer of a chloride ion by a channel that opens when glycine has been bound by the channel complex or one of its constituent parts. [GOC:mtg_transport, ISBN:0815340729]

Glycine-gated chloride ion channel activity is a fundamental process in neurotransmission, particularly in the central nervous system. This activity is mediated by specialized transmembrane proteins known as glycine receptors (GlyRs). GlyRs are pentameric ligand-gated ion channels that are activated by the neurotransmitter glycine. Glycine binding to the extracellular domain of the receptor triggers a conformational change, opening an ion pore through the membrane. This pore allows chloride ions (Cl-) to flow into the cell, leading to hyperpolarization of the neuronal membrane.

Glycine-gated chloride ion channel activity plays a crucial role in inhibitory neurotransmission. When activated, it reduces the likelihood of a postsynaptic neuron firing an action potential. This inhibitory action is essential for regulating neuronal excitability, maintaining neuronal homeostasis, and coordinating various brain functions.

Specifically, glycine-gated chloride ion channel activity is involved in:

- **Spinal cord function:** GlyRs are highly concentrated in the spinal cord, where they mediate inhibitory signals that control muscle movement and reflexes.
- **Brain function:** GlyRs are also found throughout the brain, where they are involved in various cognitive processes, including learning, memory, and sensory perception.
- **Development:** GlyRs are critical for proper neuronal development and maturation.

Dysregulation of glycine-gated chloride ion channel activity can lead to a variety of neurological disorders, including epilepsy, spasticity, and anxiety. Understanding the molecular mechanisms of glycine-gated chloride ion channel activity is therefore crucial for developing new therapies for these and other neurological conditions.'
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Proteins (1)

Compounds (2)