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神经调节蛋白β1诱导p185HER2癌蛋白的下调及泛素-蛋白酶体降解途径。

Heregulin beta1 induces the down regulation and the ubiquitin-proteasome degradation pathway of p185HER2 oncoprotein.

作者信息

Magnifico A, Tagliabue E, Ardini E, Casalini P, Colnaghi M I, Ménard S

机构信息

Division of Experimental Oncology E, Istituto Nazionale per lo Studio e la Cura dei Tumori, Milan, Italy.

出版信息

FEBS Lett. 1998 Jan 30;422(2):129-31. doi: 10.1016/s0014-5793(97)01612-8.

DOI:10.1016/s0014-5793(97)01612-8
PMID:9489990
Abstract

Analysis of the fate of the p185HER2 oncoprotein following activation by heregulin beta1 revealed the induction of the tyrosine-phosphorylation, down-modulation, and polyubiquitination of p185HER2. Receptor ubiquitination was suppressed in cells treated with heregulin beta1 in the presence of sodium azide, an inhibitor of ATP-dependent reactions, or genistein, a tyrosine kinase protein inhibitor, indicating the requirement for kinase activity and ATP in p185HER2 polyubiquitination. Ubiquitinated p185HER2 was degradated by the 26S proteasome proteolytic pathway. Kinetics and inhibition experiments indicated that endocytosis of the receptor occurs downstream of the initiation of the degradation process.

摘要

对由神经调节蛋白β1激活后的p185HER2癌蛋白的命运分析显示，p185HER2出现了酪氨酸磷酸化、下调和多聚泛素化。在叠氮化钠（一种ATP依赖性反应抑制剂）或染料木黄酮（一种酪氨酸激酶蛋白抑制剂）存在的情况下，用神经调节蛋白β1处理的细胞中，受体泛素化受到抑制，这表明p185HER2多聚泛素化需要激酶活性和ATP。泛素化的p185HER2通过26S蛋白酶体蛋白水解途径降解。动力学和抑制实验表明，受体的内吞作用发生在降解过程开始的下游。

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