Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport.
Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport.
复制标题
酵母质膜的成熟[H+] ATPase在细胞内转运过程中涉及磷酸化。
DOI：
10.1083/jcb.115.2.289
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发表时间：
1991-10
影响因子：
7.8
通讯作者：
Slayman, C W
中科院分区：
文献类型：
--
作者：
Chang, A;Slayman, C W
在这项研究中，我们表明，质膜[H+] ATP酶的酿酒酵母是磷酸化的多个丝氨酸和苏氨酸残基在体内。磷酸化发生在新合成的ATP酶从ER到细胞表面的运动过程中，如通过分析在分泌途径的连续步骤中阻断的温度敏感的sec突变体所揭示的。ATP酶的二维磷酸肽分析表明，尽管大多数位点在到达分泌囊泡时或之前被磷酸化，但一些磷酸肽是质膜所特有的。质膜特异性位点的磷酸化与葡萄糖生长期间ATP酶活性的增加有关。在葡萄糖饥饿时，去磷酸化伴随着酶活性的降低而发生，并且在再加入葡萄糖后两者都迅速逆转（在2分钟内）。我们认为，可逆的，位点特异性磷酸化作用，以调整ATP酶的活性响应营养信号。
In this study we show that the plasma membrane [H+]ATPase of Saccharomyces cerevisiae is phosphorylated on multiple Ser and Thr residues in vivo. Phosphorylation occurs during the movement of newly synthesized ATPase from the ER to the cell surface, as revealed by the analysis of temperature-sensitive sec mutants blocked at successive steps of the secretory pathway. Two-dimensional phosphopeptide analysis of the ATPase indicates that, although most sites are phosphorylated at or before arrival in secretory vesicles, some phosphopeptides are unique to the plasma membrane. Phosphorylation of plasma membrane- specific site(s) is associated with increased ATPase activity during growth on glucose. Upon glucose starvation, dephosphorylation occurs concomitantly with a decrease in enzymatic activity, and both are rapidly reversed (within 2 min) upon readdition of glucose. We suggest that reversible, site-specific phosphorylation serves to adjust ATPase activity in response to nutritional signals.