IDENTIFICATION AND ROLE OF THE BASAL PHOSPHORYLATION SITE ON HORMONE-SENSITIVE LIPASE
IDENTIFICATION AND ROLE OF THE BASAL PHOSPHORYLATION SITE ON HORMONE-SENSITIVE LIPASE
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DOI：
10.1111/j.1432-1033.1990.tb19116.x
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发表时间：
1990-07-20
期刊：
影响因子：
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通讯作者：
YEAMAN, SJ
中科院分区：
文献类型：
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作者：
GARTON, AJ;YEAMAN, SJ
牛激素敏感脂肪酶(HSL)的磷酸化位点2在体外被AMP激活的蛋白激酶磷酸化，在体外也被糖原合成酶-4磷酸化。在体外和在分离的脂肪细胞中磷酸化的HSL的多肽图谱表明，该位点对应于HSL上的基础磷酸化位点，在没有脂解刺激的情况下，该位点在完整的脂肪细胞中被磷酸化。2位点被认为具有降脂作用，因为该位点的磷酸化大大减少了随后的磷酸化(1位点)和HSL的激活，这是由环-AMP依赖的蛋白激酶引起的。使用基于1和2位点附近序列的合成肽，获得了2位点具有降脂作用的进一步证据。2位点的多肽的磷酸化完全阻止了1位点的随后的磷酸化，反之亦然。
Phosphorylation site 2 on bovine hormone-sensitive lipase (HSL), which is phosphorylated in vitro by the AMP-activated protein kinase, has been found also to be phosphorylated in vitro by glycogen synthase kinase-4. Peptide mapping of HSL phosphorylated in vitro and in isolated adipocytes demonstrates that this site corresponds to the basal phosphorylation site on HSL, which is phosphorylated in intact adipocytes in the absence of lipolytic stimuli. Site 2 has been proposed to have an antilipolytic role in that phosphorylation at this site greatly reduces subsequent phosphorylation (at site 1) and activation of HSL by cyclic-AMP-dependent protein kinase. Further evidence for an antilipolytic role of site 2 has been obtained using a synthetic peptide based on the sequence around sites 1 and 2. Phosphorylation of the peptide as site 2 totally prevents the subsequent phosphorylation of site 1 and vice versa.