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
中科院分区:
文献类型:
--
作者:
Gabriel Talaia;Christos Gournas;Elie Saliba;Cláudia Barata;M. Casal;B. André;G. Diallinas;S. Paiva
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.
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影响因子:
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