MULTISITE PHOSPHORYLATION OF GLYCOGEN-SYNTHASE FROM RABBIT SKELETAL-MUSCLE - PHOSPHORYLATION OF SITE-5 BY GLYCOGEN-SYNTHASE KINASE-5 (CASEIN KINASE-II) IS A PREREQUISITE FOR PHOSPHORYLATION OF SITES-3 BY GLYCOGEN-SYNTHASE KINASE-3
MULTISITE PHOSPHORYLATION OF GLYCOGEN-SYNTHASE FROM RABBIT SKELETAL-MUSCLE - PHOSPHORYLATION OF SITE-5 BY GLYCOGEN-SYNTHASE KINASE-5 (CASEIN KINASE-II) IS A PREREQUISITE FOR PHOSPHORYLATION OF SITES-3 BY GLYCOGEN-SYNTHASE KINASE-3
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DOI：
10.1016/0014-5793(82)81332-x
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发表时间：
1982-01-01
期刊：
影响因子：
3.5
通讯作者：
COHEN, P
中科院分区：
文献类型：
--
作者：
PICTON, C;WOODGETT, J;COHEN, P
糖原合酶激酶-5（酪蛋白激酶-II）在称为位点 5 的丝氨酸上磷酸化糖原合酶。该残基位于糖原合酶激酶-3 磷酸化的 3 个丝氨酸的 C 端，这对于体内糖原合酶的激素调节至关重要。虽然位点 5 的磷酸化不影响催化活性，但事实证明这种修饰是糖原合酶激酶 3 磷酸化的先决条件。由于位点 5 在所有条件下在体内几乎完全磷酸化，因此糖原合成酶激酶 5 在形成另一种蛋白激酶的识别位点方面似乎是一种新颖的作用
Glycogen synthase kinase‐5 (casein kinase‐II) phosphorylates glycogen synthase on a serine termed site 5. This residue is just C‐terminal to the 3 serines phosphorylated by glycogen synthase kinase‐3, which are critical for the hormonal regulation of glycogen synthase in vivo. Although phosphorylation of site 5 does not affect the catalytic activity, it is demonstrated that this modification is a prerequisite for phosphorylation by glycogen synthase kinase‐3. Since site 5 is almost fully phosphorylated in vivo under all conditions, the role of glycogen synthase kinase‐5 would appear to be a novel one in forming the recognition site for another protein kinase