The high osmolarity glycerol response (HOG) MAP kinase pathway controls localization of a yeast golgi glycosyltransferase.
The high osmolarity glycerol response (HOG) MAP kinase pathway controls localization of a yeast golgi glycosyltransferase.
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DOI：
10.1083/jcb.143.4.935
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发表时间：
1998-11-16
期刊：
影响因子：
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通讯作者：
Graham TR
中科院分区：
文献类型：
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作者：
Reynolds TB;Hopkins BD;Lyons MR;Graham TR
酵母 α-1,3-甘露糖基转移酶 (Mnn1p) 通过独立的跨膜和腔域信号定位于高尔基体。当通过将其跨膜结构域交换为可切割信号序列而表达为可溶形式 (Mnn1-s) 时，腔结构域定位于高尔基复合体（Graham, T. R., and V. A. Krasnov. 1995. Mol. Biol. Cell. 6:809–824）。通过筛选那些分泌 Mnn1-s 的诱变酵母菌落，分离出未能保留高尔基复合体中腔结构域的突变体，称为腔结构域保留 (ldr) 突变体。通过该筛选鉴定了两个基因：HOG1（一种编码丝裂原激活蛋白激酶（MAPK）的基因，在高渗透压甘油（HOG）途径中发挥作用）和LDR1。我们发现，在标准渗透条件下，需要通过 HOG 途径的基础信号传导将 Mnn1-s 定位到高尔基体。 HOG1 和 LDR1 的突变也会扰乱完整 Mnn1p 的定位，导致早期高尔基体中 Mnn1p 的丢失，并伴随着后期高尔基体中 Mnn1p 的增加。
The yeast α-1,3-mannosyltransferase (Mnn1p) is localized to the Golgi by independent transmembrane and lumenal domain signals. The lumenal domain is localized to the Golgi complex when expressed as a soluble form (Mnn1-s) by exchange of its transmembrane domain for a cleavable signal sequence (Graham, T. R., and V. A. Krasnov. 1995. Mol. Biol. Cell. 6:809–824). Mutants that failed to retain the lumenal domain in the Golgi complex, called lumenal domain retention (ldr) mutants, were isolated by screening mutagenized yeast colonies for those that secreted Mnn1-s. Two genes were identified by this screen, HOG1, a gene encoding a mitogen-activated protein kinase (MAPK) that functions in the high osmolarity glycerol (HOG) pathway, and LDR1. We have found that basal signaling through the HOG pathway is required to localize Mnn1-s to the Golgi in standard osmotic conditions. Mutations in HOG1 and LDR1 also perturb localization of intact Mnn1p, resulting in its loss from early Golgi compartments and a concomitant increase of Mnn1p in later Golgi compartments.