A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein.
A novel mechanism for localizing membrane proteins to yeast trans-Golgi network requires function of synaptojanin-like protein.
复制标题
将膜蛋白定位到酵母跨高尔基体网络的新机制需要突触贾蛋白样蛋白的功能。
DOI：
10.1091/mbc.12.10.3175
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发表时间：
2001
影响因子：
3.3
通讯作者：
Nothwehr,SF
中科院分区：
文献类型：
--
作者：
Ha,SA;Bunch,JT;Hama,H;DeWald,DB;Nothwehr,SF
Localization of resident membrane proteins to the yeasttrans-Golgi network (TGN) involves both their retrieval from a prevacuolar/endosomal compartment (PVC) and a “slow delivery” mechanism that inhibits their TGN-to-PVC transport. A screen for genes required for the slow delivery mechanism uncoveredINP53, a gene encoding a phosphoinositide phosphatase. A retrieval-defective model TGN protein, A(F→A)-ALP, was transported to the vacuole ininp53mutants approximately threefold faster than in wild type. Inp53p appears to function in a process distinct from PVC retrieval because combininginp53with mutations that block retrieval resulted in a much stronger phenotype than either mutation alone. Invps27strains defective for both anterograde and retrograde transport out of the PVC, a loss of Inp53p function markedly accelerated the rate of transport of TGN residents A-ALP and Kex2p into the PVC. Inp53p function is cargo specific because a loss of Inp53p function had no effect on the rate of Vps10p transport to the PVC invps27cells. The rate of early secretory pathway transport appeared to be unaffected ininp53mutants. Cell fractionation experiments suggested that Inp53p associates with Golgi or endosomal membranes. Taken together, these results suggest that a phosphoinositide signaling event regulates TGN-to-PVC transport of select cargo proteins.
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