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中国学者发现磷酸化p38α在蛋白酶体损伤中对细胞存活的重要作用

2016-12-20 佚名 生物谷

近日,国际神经生物学重要学术期刊Molecular Neurobiology在线发表了中科院上海生命科学研究院/上海交通大学医学院健康科学研究所乐卫东研究组的最新研究成果“A Central Role for Phosphorylated p38α in Linking Proteasome Inhibition-Induced Apoptosis and Autophagy”,揭示了磷酸化p

近日,国际神经生物学重要学术期刊Molecular Neurobiology在线发表了中科院上海生命科学研究院/上海交通大学医学院健康科学研究所乐卫东研究组的最新研究成果“A Central Role for Phosphorylated p38α in Linking Proteasome Inhibition-Induced Apoptosis and Autophagy”,揭示了磷酸化p38α在蛋白酶体损伤中对细胞存活的重要作用。

自噬和泛素蛋白酶体系统是体内两条重要的蛋白降解通路,在细胞凋亡过程中互相协作。泛素蛋白酶体损伤激活自噬,减少细胞凋亡。因此,研究蛋白酶体损伤诱导的自噬和凋亡之间的关系,以及二者之间的关键因子对于蛋白稳态失调疾病的发病机制和治疗是国际研究的热点。

乐卫东研究组成员郭芳博士发现磷酸化p38α在蛋白酶体损伤的过程中可以调节自噬进而影响细胞凋亡。通过抑制p38α的磷酸化,自噬标志蛋白LC3-II蛋白水平升高,而自噬底物SQSTM1蛋白水平降低,说明磷酸化p38α负向调控自噬;进一步研究发现,抑制p38α的磷酸化可以抑制mTOR通路从而激活自噬。而激活的自噬减少了细胞凋亡。

该研究阐述了磷酸化p38α,在蛋白酶体损伤模型中自噬和凋亡之间的重要作用,为研究自噬和凋亡之间的关系提供了新的思路。同时,该研究还提供了一个新的自噬激活和细胞凋亡的分子靶点。

此课题研究得到了国家自然科学基金委和中国科学院等经费资助。

原始出处

Guo F1, He XB2, Li S3, Le W4,5,6.A Central Role for Phosphorylated p38α in Linking Proteasome Inhibition-Induced Apoptosis and Autophagy.Mol Neurobiol. 2016 Nov 10.

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    2017-07-18 DEXTER3139
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