Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domain.
Golgi-to-late endosome trafficking of the yeast pheromone processing enzyme Ste13p is regulated by a phosphorylation site in its cytosolic domain.
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酵母信息素加工酶 Ste13p 的高尔基体到晚期内体的运输受到其胞质结构域中的磷酸化位点的调节。
DOI：
10.1091/mbc.e04-07-0642
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发表时间：
2005
影响因子：
3.3
通讯作者：
Nothwehr,StevenF
中科院分区：
文献类型：
--
作者：
Johnston,HollyD;Foote,Christopher;Santeford,Andrea;Nothwehr,StevenF
This study addressed whether phosphorylation regulates trafficking of yeast membrane proteins that cycle between thetrans-Golgi network (TGN) and endosomal system. The TGN membrane proteins A-ALP, a model protein containing the Ste13p cytosolic domain fused to alkaline phosphatase (ALP), and Kex2p were found to be phosphorylated in vivo. Mutation of the S13residue on the cytosolic domain of A-ALP to Ala was found to block trafficking to the prevacuolar compartment (PVC), whereas a S13D mutation generated to mimic phosphorylation accelerated trafficking into the PVC. The S13residue was shown by mass spectrometry to be phosphorylated. The rate of endoplasmic reticulum-to-Golgi transport of newly synthesized A(S13A)-ALP was indistinguishable from wild-type, indicating that the lack of transport of A(S13A)-ALP to the PVC was instead due to differences in Golgi/endosomal trafficking. The A(S13A)-ALP protein exhibited a TGN-like localization similar to that of wild-type A-ALP. Similarly, the S13A mutation in endogenous Ste13p did not reduce the extent of or longevity of its localization to the TGN as shown by α-factor processing assays. These results indicate that S13phosphorylation is required for TGN-to-PVC trafficking of A-ALP and imply that phosphorylation of S13may regulate recognition of A-ALP by vesicular trafficking machinery.
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