Transporters of the solute carrier 6 (SLC6) family mediate the reuptake of neurotransmitters such as dopamine, norepinephrine, serotonin, GABA, and glycine. SLC6 family members are 12 transmembrane helix-spanning proteins that operate using the transmembrane sodium gradient for transport. These transporters assume various quaternary arrangements ranging from monomers to complex stoichiometries with multiple subunits. Dopamine and serotonin transporter oligomerization has been implicated in trafficking of newly formed proteins from the endoplasmic reticulum to the plasma membrane with a pre-fixed assembly. Once at the plasma membrane, oligomers are kept fixed in their quaternary assembly by interaction with phosphoinositides. While it remains unclear how oligomer formation precisely affects physiological transporter function, it has been shown that oligomerization supports the activity of release-type psychostimulants. Most recently, single molecule microscopy experiments unveiled that the stoichiometry differs between individual members of the SLC6 family. The present overview summarizes our understanding of the influence of plasma membrane constituents on transporter oligomerization, describes the known interfaces between protomers and discusses open questions.

中文翻译：

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SLC6 转运蛋白寡聚化

溶质载体 6 (SLC6) 家族的转运蛋白介导多巴胺、去甲肾上腺素、血清素、GABA 和甘氨酸等神经递质的再摄取。SLC6 家族成员是 12 个跨膜螺旋跨越蛋白，它们使用跨膜钠梯度进行转运。这些转运蛋白采用各种四元排列，从单体到具有多个亚基的复杂化学计量。多巴胺和5-羟色胺转运蛋白寡聚化与新形成的蛋白质从内质网到具有预先固定组件的质膜的运输有关。一旦在质膜上，寡聚体通过与磷酸肌醇的相互作用被固定在它们的四元组装体中。虽然目前尚不清楚寡聚体形成如何精确影响生理转运蛋白功能，已经表明，寡聚化支持释放型精神兴奋剂的活性。最近，单分子显微镜实验揭示了 SLC6 家族的各个成员之间的化学计量不同。本概述总结了我们对质膜成分对转运蛋白寡聚化影响的理解，描述了原体之间已知的界面并讨论了开放性问题。