TARGET OF RAPAMYCIN IN YEAST, TOR2, IS AN ESSENTIAL PHOSPHATIDYLINOSITOL KINASE HOMOLOG REQUIRED FOR G(1) PROGRESSION
TARGET OF RAPAMYCIN IN YEAST, TOR2, IS AN ESSENTIAL PHOSPHATIDYLINOSITOL KINASE HOMOLOG REQUIRED FOR G(1) PROGRESSION
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DOI：
10.1016/0092-8674(93)90144-f
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发表时间：
1993-05-07
期刊：
影响因子：
64.5
通讯作者：
HALL, MN
中科院分区：
文献类型：
--
作者：
KUNZ, J;HENRIQUEZ, R;HALL, MN
酵母TOR 2基因编码一个必需的282 kd磷脂酰肌醇（PI）3-激酶同源物。TOR 2与牛PI 3-激酶的催化亚基和酵母VPS 34相关，VPS 34是一种空泡分选蛋白，也显示具有PI 3-激酶活性。免疫抑制剂雷帕霉素最有可能通过抑制PI激酶活性起作用，因为TOR 2突变赋予雷帕霉素抗性，并且因为TOR 1 TOR 2双破坏（TOR 1是非必需的TOR 2同源物）赋予G1阻滞，雷帕霉素也是如此。我们的研究结果进一步表明，3-磷酸化的磷酸肌醇，其生理意义尚未确定，是一个重要的信号在细胞周期激活。在酵母中，该信号可能在类似于T细胞中的白细胞介素-2信号转导途径的信号转导途径中起作用。
The yeast TOR2 gene encodes an essential 282 kd phosphatidylinositol (PI) 3-kinase homolog. TOR2 is related to the catalytic subunit of bovine PI 3-kinase and to yeast VPS34, a vacuolar sorting protein also shown to have PI 3-kinase activity. The immunosuppressant rapamycin most likely acts by inhibiting PI kinase activity because TOR2 mutations confer resistance to rapamycin and because a TOR1 TOR2 double disruption (TOR1 is a nonessential TOR2 homolog) confers G1 arrest, as does rapamycin. Our results further suggest that 3-phosphorylated phosphoinositides, whose physiological significance has not been determined, are an important signal in cell cycle activation. In yeast, this signal may act in a signal transduction pathway similar to the interleukin-2 signal transduction pathway in T cells.