Literature DB >> 12351715

Coupled and uncoupled gating and desensitization effects by pore domain mutations in GABA(A) receptors.

Michaela Scheller1, Stuart A Forman.   

Abstract

GABA(A) receptors are allosteric ligand-gated ion channels. Agonist-induced gating and desensitization have been proposed to be coupled via pore domain structures. Mutations at two alpha1 subunit pore-domain (transmembrane domain 2) residues enhance GABA sensitivity, leucine-to-threonine at position 264 (9'), and serine-to-isoleucine at position 270 (15'). We investigated the role of these residues in gating, desensitization, and deactivation of alpha1beta2gamma2L GABA(A) receptors using rapid GABA concentration jumps and patch-clamp electrophysiology. GABA EC(50) values for alpha1(L264T)beta2gamma2L and alpha1(S270I)beta2gamma2L currents were, respectively, approximately 80-fold and 13-fold lower than the wild-type EC50. Unlike wild type, both mutant receptors displayed significant picrotoxin-sensitive currents in the absence of GABA, indicating that they enhance gating efficacy. Both mutants displayed current activation rates that matched wild type at 1 microm GABA and above. Desensitization of wild-type and alpha1(S270I)beta2gamma2L currents displayed indistinguishable rates and amplitudes, whereas alpha1(L264T)beta2gamma2L currents desensitized extremely slowly. Deactivation of wild-type currents displayed two rates and slowed after partial desensitization, whereas currents from both mutants deactivated slowly with single rate constants that were unaffected by desensitization. These results indicate that both alpha1(L264T) and alpha1(S270I) mutations increase the gating efficacy of receptors by slowing channel closing, which accounts for nearly all of the similar changes that they produce in macrocurrent dynamics. Because the alpha1(S270I) mutation uncouples its gating effects from those on rapid desensitization, these two processes are necessarily associated with movements of distinct receptor structures (gates). The effects of the alpha1(L264T) mutation suggest that the conserved leucines may play a role in gating-desensitization coupling.

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Year:  2002        PMID: 12351715      PMCID: PMC6757762     

Source DB:  PubMed          Journal:  J Neurosci        ISSN: 0270-6474            Impact factor:   6.167


  37 in total

1.  Use of the covariance matrix in directly fitting kinetic parameters: application to GABAA receptors.

Authors:  James J Celentano; Alan G Hawkes
Journal:  Biophys J       Date:  2004-07       Impact factor: 4.033

2.  An arginine involved in GABA binding and unbinding but not gating of the GABA(A) receptor.

Authors:  David A Wagner; Cynthia Czajkowski; Mathew V Jones
Journal:  J Neurosci       Date:  2004-03-17       Impact factor: 6.167

3.  Activation of single heteromeric GABA(A) receptor ion channels by full and partial agonists.

Authors:  Martin Mortensen; Uffe Kristiansen; Bjarke Ebert; Bente Frølund; Povl Krogsgaard-Larsen; Trevor G Smart
Journal:  J Physiol       Date:  2004-02-27       Impact factor: 5.182

4.  Effects of ethanol on adenosine 5'-triphosphate-gated purinergic and 5-hydroxytryptamine receptors.

Authors:  Daryl L Davies; Liana Asatryan; Sacha T Kuo; John J Woodward; Brian F King; Ronald L Alkana; Cheng Xiao; Jiang Hong Ye; Hui Sun; Li Zhang; Xiang-Qun Hu; Volodya Hayrapetyan; David M Lovinger; Tina K Machu
Journal:  Alcohol Clin Exp Res       Date:  2006-02       Impact factor: 3.455

5.  Kinetics of anesthetic-induced conformational transitions in a four-alpha-helix bundle protein.

Authors:  Ken Solt; Jonas S Johansson; Douglas E Raines
Journal:  Biochemistry       Date:  2006-02-07       Impact factor: 3.162

6.  Microscopic kinetic determinants of macroscopic currents: insights from coupling and uncoupling of GABAA receptor desensitization and deactivation.

Authors:  Matt T Bianchi; Emmanuel J Botzolakis; Kevin F Haas; Janet L Fisher; Robert L Macdonald
Journal:  J Physiol       Date:  2007-09-20       Impact factor: 5.182

7.  Tryptophan mutations at azi-etomidate photo-incorporation sites on alpha1 or beta2 subunits enhance GABAA receptor gating and reduce etomidate modulation.

Authors:  Deirdre Stewart; Rooma Desai; Qi Cheng; Aiping Liu; Stuart A Forman
Journal:  Mol Pharmacol       Date:  2008-09-19       Impact factor: 4.436

8.  A residue in loop 9 of the beta2-subunit stabilizes the closed state of the GABAA receptor.

Authors:  Carrie A Williams; Shannon V Bell; Andrew Jenkins
Journal:  J Biol Chem       Date:  2009-12-10       Impact factor: 5.157

9.  Photo-activated azi-etomidate, a general anesthetic photolabel, irreversibly enhances gating and desensitization of gamma-aminobutyric acid type A receptors.

Authors:  Huijun Zhong; Dirk Rüsch; Stuart A Forman
Journal:  Anesthesiology       Date:  2008-01       Impact factor: 7.892

10.  State-dependent etomidate occupancy of its allosteric agonist sites measured in a cysteine-substituted GABAA receptor.

Authors:  Deirdre S Stewart; Mayo Hotta; Rooma Desai; Stuart A Forman
Journal:  Mol Pharmacol       Date:  2013-03-22       Impact factor: 4.436

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