PNAS:香港科技大学夏军课题组揭示PICK1能有效抑制帕金森,降低其自我保护能力

2018-07-11 生态平衡 iNature

2018年7月9日,香港科技大学生命科学系夏军研究组在PNAS上发表题为“PICK1 inhibits the E3 ubiquitin ligase activity of Parkin and reduces itsneuronal protective effect”的文章。在这里,研究人员发现与PRKCA1(PICK1)相互作用的蛋白质的Bin / Amphiphysin / Rvs(BA

2018年7月9日,香港科技大学生命科学系夏军研究组在PNAS上发表题为“PICK1 inhibits the E3 ubiquitin ligase activity of Parkin and reduces itsneuronal protective effect”的文章。在这里,研究人员发现与PRKCA1(PICK1)相互作用的蛋白质的Bin / Amphiphysin / Rvs(BAR)结构域与Parkin的(RING1)结构域结合,并通过破坏其与UbcH7的相互作用而有效抑制Parkin的E3连接酶活性。该研究表明PICK1是帕金森的有效抑制剂,并且PICK1的减少增强了对帕金森的保护作用。

帕金森病(PD)是第二种最常见的神经退行性疾病。其特征在于由多巴胺产生神经元的丧失引起的运动功能的进行性恶化。目前,没有任何治疗可以阻止疾病的进展。 Parkin中的功能丧失突变占早发性PD的约50%。 Parkin作为E3泛素连接酶发挥作用,尤其在多巴胺能神经元中具有多重保护作用。在这里,我们证明PICK1直接与Parkin结合。 PICK1是Parkin E3泛素连接酶活性的有效内源性抑制剂,可阻断Parkin的保护功能。相反,PICK1的敲除增强了Parkin的神经保护作用。因此,PICK1的减少可以提供治疗PD的治疗靶标。

Parkin作为多功能E3泛素连接酶起作用,并且Parkin功能丧失与散发性和家族性帕金森病(PD)相关。我们报道,与PRKCA1(PICK1)相互作用的蛋白质的Bin / Amphiphysin / Rvs(BAR)结构域与Parkin真正有趣的新基因1(RING1)结构域结合,并通过破坏其与UbcH7的相互作用而有效抑制Parkin的E3连接酶活性。 Parkin易位至受损的线粒体并导致其在神经元中降解,而PICK1强烈抑制该过程。 PICK1还损害了Parkin对SH-SY5Y细胞和神经元中的应激的保护功能。在年轻的PICK1敲除小鼠中,几种Parkin底物的蛋白质水平降低,并且这些小鼠对1-甲基-4-苯基-1,2,3,6-四氢吡啶(MPTP)介导的毒性具有抗性。总之,结果表明PICK1是帕金的有效抑制剂,并且PICK1的减少增强了帕金的保护作用。

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    2018-11-15 zhlpower
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    2018-12-24 docwu2019
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    2018-07-20 wxl882001

    学习一下

    0

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    2018-07-12 kafei

    学习学习谢谢

    0

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