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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Glycine residues G338 and G342 are important determinants for serotonin transporter dimerisation and cell surface expression.
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Glycine residues G338 and G342 are important determinants for serotonin transporter dimerisation and cell surface expression.

机译：甘氨酸残基G338和G342是血清素转运蛋白二聚化和细胞表面表达的重要决定因素。

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摘要

Compelling evidence has been provided that Na(+) and Cl(-)-dependent neurotransmitter transporter proteins form oligomeric complexes. Specific helix-helix interactions in lipid bilayers are thought to promote the assembly of integral membrane proteins to oligomeric structures. These interactions are determined by selective transmembrane helix packing motifs one of which is the Glycophorin A motif (GxxxG). This motif is present in the sixth transmembrane domain of most transporter proteins. In order to investigate, whether this motif is important for proper expression and function of the serotonin transporter (SERT), we have analysed the effect of mutating the respective glycine residues Gly338 and Gly342 to valine upon transient expression of the respective cDNAs in HEK293 cells. As revealed by western blotting, wildtype SERT is found in monomeric and dimeric forms while both mutants are expressed as monomers solely. Confocal microscopy revealed that the wildtype SERT is expressed at the cell surface, whereas both mutant proteins are localised in intracellular compartments. Failure of integration into the cell membrane is responsible for a total loss of [(3)H]5HT uptake capability by the mutants. These findings show that in the SERT protein the integrity of the GxxxG motif is essential for dimerisation and proper targeting of the transporter complex to the cell surface.
机译：提供了令人信服的证据，即Na（+）和Cl（-）依赖性神经递质转运蛋白形成寡聚复合物。脂质双层中的特定螺旋-螺旋相互作用被认为促进整合膜蛋白组装为寡聚结构。这些相互作用是由选择性跨膜螺旋堆积基序确定的，其中一个是糖蛋白A基序（GxxxG）。该基序存在于大多数转运蛋白的第六个跨膜结构域中。为了研究该基序对于5-羟色胺转运蛋白（SERT）的正确表达和功能是否重要，我们分析了在HEK293细胞中各个cDNA瞬时表达后，将各个甘氨酸残基Gly338和Gly342突变为缬氨酸的作用。如通过蛋白质印迹所揭示的，发现野生型SERT以单体和二聚体形式存在，而两个突变体仅被表达为单体。共聚焦显微镜显示野生型SERT在细胞表面表达，而两种突变蛋白均位于细胞内区室。整合到细胞膜中的失败是突变体完全丧失[（3）H] 5HT摄取能力的原因。这些发现表明，在SERT蛋白中，GxxxG基序的完整性对于二聚化和将转运蛋白复合物正确靶向细胞表面至关重要。

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