PHAS-1 AS A LINK BETWEEN MITOGEN-ACTIVATED PROTEIN-KINASE AND TRANSLATION INITIATION
PHAS-1 AS A LINK BETWEEN MITOGEN-ACTIVATED PROTEIN-KINASE AND TRANSLATION INITIATION
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DOI：
10.1126/science.7939721
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发表时间：
1994-10-28
期刊：
影响因子：
56.9
通讯作者：
LAWRENCE, JC
中科院分区：
文献类型：
--
作者：
LIN, TA;KONG, XM;LAWRENCE, JC
PHAS-I是在许多组织中发现的热稳定蛋白质（相对分子质量约为12，400）。在与胰岛素或生长因子孵育的大鼠脂肪细胞中迅速磷酸化。非磷酸化的PHAS-I与起始因子4 E（eIF-4 E）结合并抑制蛋白质合成。丝氨酸-64在PHAS-I迅速磷酸化的有丝分裂原激活（MAP）激酶，主要的胰岛素刺激的PHAS-I激酶在脂肪细胞提取物。用抗体、固定的PHAS-I和信使RNA帽亲和树脂获得的结果表明，当丝氨酸-64被磷酸化时，PHAS-I不结合eIF-4 E。因此，PHAS-I可能是激活MAP激酶的不同试剂和刺激物组刺激蛋白质合成的关键介体。
PHAS-I is a heat-stable protein (relative molecular mass approximate to 12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.