Multifunctional basic motif in the glycine receptor intracellular domain induces subunit-specific sorting.

Melzer, N., Villman, C., Becker, K., Harvey, K., Harvey, R.J., Vogel, N., Kluck, C.J., Kneussel, M. and Becker, C.M. (2010) Multifunctional basic motif in the glycine receptor intracellular domain induces subunit-specific sorting. Journal of Biological Chemistry, 285 (6). pp. 3730-3739. 10.1074/jbc.M109.030460 .

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Official URL: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2823514

DOI: 10.1074/jbc.M109.030460

Abstract

The strychnine-sensitive glycine receptor (GlyR) is a ligand-gated ion channel that mediates fast synaptic inhibition in the vertebrate central nervous system. As a member of the family of Cys-loop receptors, it assembles from five homologous subunits (GlyRalpha1-4 and -beta). Each subunit contains an extracellular ligand binding domain, four transmembrane domains (TM), and an intracellular domain, formed by the loop connecting TM3 and TM4 (TM3-4 loop). The TM3-4 loops of the subunits GlyRalpha1 and -alpha3 harbor a conserved basic motif, which is part of a potential nuclear localization signal. When tested for functionality by live cell imaging of green fluorescent protein and beta-galactosidase-tagged domain constructs, the TM3-4 loops of GlyRalpha1 and -alpha3, but not of GlyRalpha2 and -beta, exhibited nuclear sorting activity. Subunit specificity may be attributed to slight amino acid alterations in the basic motif. In yeast two-hybrid screening and GST pulldown assays, karyopherin alpha3 and alpha4 were found to interact with the TM3-4 loop, providing a molecular mechanism for the observed intracellular trafficking. These results indicate that the multifunctional basic motif of the TM3-4 loop is capable of mediating a karyopherin-dependent intracellular sorting of full-length GlyRs.

Item Type:Article
Additional Information:Full text available electronically from the School of Pharmacy Library.
Departments, units and centres:Department of Pharmacology > Department of Pharmacology
ID Code:1328
Journal or Publication Title:Journal of Biological Chemistry
Deposited By:Library Staff
Deposited On:04 Aug 2010 10:21
Last Modified:06 Oct 2011 16:01

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