Glycine receptor

Glycine receptor

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.

Activation and inactivation

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. cite journal | last =Rajendra | first =S | authorlink = | coauthors =Lynch JW, Schofield PR | title =The glycine receptor | journal =Pharmacology and Therapeutics | volume =73 | issue =2 | pages =121–146 | publisher = | date =1997 | url =http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9131721 | doi = 10.1016/S0163-7258(96)00163-5| pmid =9131721 | accessdate =2007-01-16 ]

Arrangement of subunits

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.cite journal | last =Miyazawa | first =A | authorlink = | coauthors =Fujiyoshi Y, Unwin N | title =Structure and gating mechanism of the acetylcholine receptor pore | journal = Nature| volume =423 | issue =6943 | pages = 949–955| publisher = | date =2003 | url = | doi = 10.1038/nature01748| pmid =12827192 | accessdate = ]

There are presently four known isoforms of the α-subunit (α1-4) of GlyR that are essential to bind ligands (Gene|GLRA1, Gene|GLRA2, Gene|GLRA3, Gene|GLRA4) and a single β-subunit (Gene|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 subunitscite journal | last =Kuhse | first = J| authorlink = | coauthors = Laube B, Magalei D, Betz H| title =Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry | journal =Neuron | volume =11 | issue =6 | pages =1049–1056 | publisher = | date =1993 | url = | doi = 10.1016/0896-6273(93)90218-G| pmid =8274276 | accessdate = ] or four α1 subunits and one β subunit.cite journal | last =Kuhse | first =J | authorlink = | coauthors =Betz H, Kirsch J | title =The inhibitory glycine receptor: architecture, synaptic localization and molecular pathology of a postsynaptic ion-channel complex | journal =Current Opinion in Neurobiology | volume =5 | issue =3 | pages =318–323 | publisher = | date =1995 | url = | doi = 10.1016/0959-4388(95)80044-1| pmid =7580154 | accessdate = ] 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, and the α1 homomeric receptor is essential for studies of channel pharmacokinetics and pharmacodynamics.cite journal | last = Lewis | first =TM | authorlink = | coauthors =Schofield PR, McClellan AM | title =Kinetic determinants of agonist action at the recombinant human glycine receptor | journal =Journal of Physiology | volume =549 | issue =Part 2 | pages =361–374 | publisher = | date =2003 | url =http://jp.physoc.org/cgi/content/full/549/2/361 | doi = 10.1113/jphysiol.2002.037796| pmid =12679369 | accessdate =2007-01-16 ]

Pathology

A mutation in GLRA1 is responsible for some cases of stiff person syndrome. [OMIM|184850|STIFF-PERSON SYNDROME; SPS]

Research

Quantum dots have been used to track the diffusion of glycine receptors into the synapse of neurons. [cite journal |author=Dahan M, Lévi S, Luccardini C, Rostaing P, Riveau B, Triller A |title=Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking |journal=Science |volume=302 |issue=5644 |pages=442–5 |year=2003 |pmid=14564008 |doi=10.1126/science.1088525]

References

External links

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