The α-Arrestin Bul1p Mediates Lactate Transporter Endocytosis in Response to Alkalinization and Distinct Physiological Signals.

The α-Arrestin Bul1p Mediates Lactate Transporter Endocytosis in Response to Alkalinization and Distinct Physiological Signals.
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α-Arrestin Bul1p 介导乳酸转运蛋白内吞作用以响应碱化和不同的生理信号。

DOI:
10.1016/j.jmb.2017.09.014
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发表时间:
2017
影响因子:
5.6
通讯作者:
S. Paiva
S. Paiva
中科院分区:
生物学2区
文献类型:
--
作者:
Gabriel Talaia;Christos Gournas;Elie Saliba;Cláudia Barata;M. Casal;B. André;G. Diallinas;S. Paiva

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真核α-抑制蛋白将环境或应激信号通路与质膜转运蛋白或受体的内吞作用连接起来。酿酒酵母乳酸转运蛋白Jen 1 p已被用作阐明内吞周转响应碳源的机制的模型货物。在这里,我们发现了一个新的途径Jen 1 p的内吞作用介导的α-抑制蛋白Bul 1 p在放线菌酮或雷帕霉素的存在下,或在乳酸的延长生长。虽然放线菌酮或雷帕霉素修饰细胞多效性,乳酸盐中的长期生长的主要影响被证明是外部pH碱化。重要的是,雇用特定的非活性Jen 1 p版本表明,Bul 1 p依赖的内吞作用需要乳酸转运,根据施加的信号。我们的研究结果支持一个模型,其中Jen 1 p的构象变化,与基板/H+同向转运,是至关重要的Bul 1 p依赖Jen 1 p营业额的效率。
Eukaryotic α-arrestins connect environmental or stress signaling pathways to the endocytosis of plasma membrane transporters or receptors. The Saccharomyces cerevisiae lactate transporter Jen1p has been used as a model cargo for elucidating the mechanisms underlying endocytic turnover in response to carbon sources. Here, we discover a novel pathway of Jen1p endocytosis mediated by the α-arrestin Bul1p in response to the presence of cycloheximide or rapamycin, or prolonged growth in lactate. While cycloheximide or rapamycin modify cells pleiotropically, the major effect of prolonged growth in lactate was shown to be external pH alkalinization. Importantly, employment of specific inactive Jen1p versions showed that Bul1p-dependent endocytosis requires lactate transport, according to the signal imposed. Our results support a model where conformational changes of Jen1p, associated with substrate/H+symport, are critical for the efficiency of Bul1p-dependent Jen1p turnover.
硫氧还蛋白相互作用蛋白的翻译后调节。
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