Arrestin-Mediated Endocytosis of Yeast Plasma Membrane Transporters
Arrestin-Mediated Endocytosis of Yeast Plasma Membrane Transporters
复制标题
DOI：
10.1111/j.1600-0854.2009.00990.x
复制
发表时间：
2009-12-01
期刊：
影响因子：
4.5
通讯作者：
Pelham, Hugh R. B.
中科院分区：
文献类型：
--
作者：
Nikko, Elina;Pelham, Hugh R. B.
酵母中的许多质膜转运蛋白在过量底物或某些胁迫下被内吞，并在液泡中降解。内吞作用总是需要HECT结构域连接酶Rsp 5的泛素化。在锰转运蛋白Smf 1和氨基酸转运蛋白Can 1、Lyp 1和Mup 1的情况下，已经表明泛素化是由与Rsp 5结合并识别特定转运蛋白的抑制蛋白样衔接蛋白介导的。由于酵母含有一个大家族的arrestins，这已被建议作为一个通用的模式，转运调控，然而，分析是复杂的冗余arrestins之间。我们已经通过去除所有的抑制蛋白并检查另外四种转运蛋白Itr 1（肌醇）、Hxt 6（葡萄糖）、Fur 4（尿嘧啶）和Tat 2（色氨酸）的内吞作用的要求来测试该模型。这揭示了抑制蛋白Art 5/Ygr 068 c和Art 4/Rod 1的功能，以及Art 1/Ldb 19、Art 2/Ecm 21和Art 8/Csr 2的其他作用。它还揭示了抑制蛋白和抑制蛋白样衔接子Bul 1和Bul 2之间的功能冗余。此外，我们表明，传递到液泡往往需要多个额外的泛素连接酶或衔接子，包括环结构域连接酶Pib 1，和衔接子Bsd 2，Ear 1和Ssh 4，一些作用冗余。我们讨论了不同转运体监管要求的相似性和差异。
Many plasma membrane transporters in yeast are endocytosed in response to excess substrate or certain stresses and degraded in the vacuole. Endocytosis invariably requires ubiquitination by the HECT domain ligase Rsp5. In the cases of the manganese transporter Smf1 and the amino acid transporters Can1, Lyp1 and Mup1 it has been shown that ubiquitination is mediated by arrestin-like adaptor proteins that bind to Rsp5 and recognize specific transporters. As yeast contains a large family of arrestins, this has been suggested as a general model for transporter regulation; however, analysis is complicated by redundancy amongst the arrestins. We have tested this model by removing all the arrestins and examining the requirements for endocytosis of four more transporters, Itr1 (inositol), Hxt6 (glucose), Fur4 (uracil) and Tat2 (tryptophan). This reveals functions for the arrestins Art5/Ygr068c and Art4/Rod1, and additional roles for Art1/Ldb19, Art2/Ecm21 and Art8/Csr2. It also reveals functional redundancy between arrestins and the arrestin-like adaptors Bul1 and Bul2. In addition, we show that delivery to the vacuole often requires multiple additional ubiquitin ligases or adaptors, including the RING domain ligase Pib1, and the adaptors Bsd2, Ear1 and Ssh4, some acting redundantly. We discuss the similarities and differences in the requirements for regulation of different transporters.