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The glycine receptor, or GlyR, is the receptor for the amino acid neurotransmitter glycine. It is one of the most widely distributed inhibitory receptors in the central nervous system and has important roles in a variety of physiological processes, especially in mediating inhibitory neurotransmission in the spinal cord and brain stem.[1]

Activation and inactivationEdit

The receptor can be activated by a range of simple amino acids including glycine, β-alanine and taurine, and can be selectively blocked by the high-affinity competitive antagonist strychnine.[2]

Arrangement of subunitsEdit

Strychnine-sensitive glycine receptors are members of a family of Ligand-gated ion channels. Receptors of this family are arranged as five subunits surrounding a central pore, with each subunit composed of four α helical transmembrane segments.[3]

There are presently four known isoforms of the α-subunit (α1-4) of GlyR that are essential to bind ligands (GLRA1, GLRA2, GLRA3, GLRA4) and a single β-subunit (GLRB).

The adult form of the GlyR is the heteromeric α1β receptor, which is believed to have a stoichiometry (proportion) of three α1 subunits and two β subunits [4] or four α1 subunits and one β subunit.[5] The α-subunits are also able to form functional homo-pentameric receptors in heterologous expression systems in African clawed frog's oocytes or mammalian cell lines,[5] and the α1 homomeric receptor is essential for studies of channel pharmacokinetics and pharmacodynamics.[6]

Glycine receptors in DiseaseEdit

A disruption GlyR surface expression or by reducing the ability of expressed GlyRs to conduct chloride ions results in the rare neurological disorder, hyperekplexia. The disorder is characterized by an exaggerated response to unexpected stimuli which is followed by a temporary but complete muscular rigidity often resulting in an unprotected fall. Chronic injuries as a result of the falls are symptomatic of the disorder.[1] A mutation in GLRA1 is responsible for some cases of stiff person syndrome.[7]


Quantum dots have been used to track the diffusion of glycine receptors into the synapse of neurons.[8]


  1. 1.0 1.1 Lynch JW (October 2004). Molecular structure and function of the glycine receptor chloride channel. Physiological reviews 84 (4): 1051–95.
  2. Rajendra, S, Lynch JW, Schofield PR (1997). The glycine receptor. Pharmacology and Therapeutics 73 (2): 121–146.
  3. Miyazawa, A, Fujiyoshi Y, Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (6943): 949–955.
  4. Kuhse, J, Laube B, Magalei D, Betz H (1993). Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry. Neuron 11 (6): 1049–1056.
  5. 5.0 5.1 Kuhse, J, Betz H, Kirsch J (1995). The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex. Current Opinion in Neurobiology 5 (3): 318–323.
  6. Lewis, TM, Schofield PR, McClellan AM (2003). Kinetic determinants of agonist action at the recombinant human glycine receptor. Journal of Physiology 549 (Part 2): 361–374.
  7. OMIM 184850
  8. Dahan M, Lévi S, Luccardini C, Rostaing P, Riveau B, Triller A (2003). Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302 (5644): 442–5.

External linksEdit

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