Literature DB >> 15919190

How did the neurotransmitter cross the bilayer? A closer view.

Mark S Sonders1, Matthias Quick, Jonathan A Javitch.   

Abstract

Plasma membrane neurotransmitter transporters for monoamines, GABA, glycine and excitatory amino acids are homologous to two sizable families of bacterial amino acid transporters. Recently, a high resolution structure was determined for a thermophilic glutamate transporter. Also, a bacterial tryptophan transporter related to the family of biogenic amine neurotransmitter transporters was functionally expressed. Structural insights from these and other bacterial transporters will help to rationalize the mechanisms for the increasingly complex functions that have been described for mammalian transporters, in addition to their modes of regulation. We touch on recent insights into the functions of neurotransmitter transporters in their physiological contexts.

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Year:  2005        PMID: 15919190     DOI: 10.1016/j.conb.2005.05.009

Source DB:  PubMed          Journal:  Curr Opin Neurobiol        ISSN: 0959-4388            Impact factor:   6.627


  13 in total

1.  The mechanism of a neurotransmitter:sodium symporter--inward release of Na+ and substrate is triggered by substrate in a second binding site.

Authors:  Lei Shi; Matthias Quick; Yongfang Zhao; Harel Weinstein; Jonathan A Javitch
Journal:  Mol Cell       Date:  2008-06-20       Impact factor: 17.970

Review 2.  The sodium/multivitamin transporter: a multipotent system with therapeutic implications.

Authors:  Matthias Quick; Lei Shi
Journal:  Vitam Horm       Date:  2015-03-07       Impact factor: 3.421

3.  Identification and characterization of 3-iodothyronamine intracellular transport.

Authors:  Alexandra G Ianculescu; Kathleen M Giacomini; Thomas S Scanlan
Journal:  Endocrinology       Date:  2008-12-12       Impact factor: 4.736

4.  Single-molecule dynamics of gating in a neurotransmitter transporter homologue.

Authors:  Yongfang Zhao; Daniel Terry; Lei Shi; Harel Weinstein; Scott C Blanchard; Jonathan A Javitch
Journal:  Nature       Date:  2010-05-13       Impact factor: 49.962

5.  Conformational changes in dopamine transporter intracellular regions upon cocaine binding and dopamine translocation.

Authors:  Yvette Dehnes; Jufang Shan; Thijs Beuming; Lei Shi; Harel Weinstein; Jonathan A Javitch
Journal:  Neurochem Int       Date:  2014-02-24       Impact factor: 3.921

6.  The cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.

Authors:  Sayan Mondal; George Khelashvili; Lei Shi; Harel Weinstein
Journal:  Chem Phys Lipids       Date:  2013-01-30       Impact factor: 3.329

Review 7.  Unlocking the molecular secrets of sodium-coupled transporters.

Authors:  Harini Krishnamurthy; Chayne L Piscitelli; Eric Gouaux
Journal:  Nature       Date:  2009-05-21       Impact factor: 49.962

8.  Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT.

Authors:  Chunfeng Zhao; Sebastian Stolzenberg; Luis Gracia; Harel Weinstein; Sergei Noskov; Lei Shi
Journal:  Biophys J       Date:  2012-09-05       Impact factor: 4.033

9.  The LeuT-fold neurotransmitter:sodium symporter MhsT has two substrate sites.

Authors:  Matthias Quick; Ara M Abramyan; Pattama Wiriyasermkul; Harel Weinstein; Lei Shi; Jonathan A Javitch
Journal:  Proc Natl Acad Sci U S A       Date:  2018-08-06       Impact factor: 11.205

10.  Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation.

Authors:  Matthias Quick; Anne-Marie Lund Winther; Lei Shi; Poul Nissen; Harel Weinstein; Jonathan A Javitch
Journal:  Proc Natl Acad Sci U S A       Date:  2009-03-23       Impact factor: 11.205

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