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论文题目: AMPK regulates autophagy by phosphorylating BECN1 at threonine 388
英文论文题目: AMPK regulates autophagy by phosphorylating BECN1 at threonine 388
第一作者: Zhang, DY; Wang, W; Sun, XJ; Xu, DQ; Wang, CY; Zhang, Q; Wang, HF; Luo, WW; Chen, Y; Chen, HY; Liu, ZX
英文第一作者: Zhang, DY; Wang, W; Sun, XJ; Xu, DQ; Wang, CY; Zhang, Q; Wang, HF; Luo, WW; Chen, Y; Chen, HY; Liu, ZX
联系作者: Liu, ZX (reprint author), Shanghai Inst Biol Sci, Inst Nutr Sci, 320 Yueyang RD Life Sci Bldg RM A2012, Shanghai 200031, Peoples R China.
英文联系作者: Liu, ZX (reprint author), Shanghai Inst Biol Sci, Inst Nutr Sci, 320 Yueyang RD Life Sci Bldg RM A2012, Shanghai 200031, Peoples R China.
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发表年度: 2016
卷: 12
期: 9
页码: 1447-1459
摘要: Macroautophagy/autophagy is a conserved catabolic process that recycles cytoplasmic material during low energy conditions. BECN1/Beclin1 (Beclin 1, autophagy related) is an essential protein for function of the class 3 phosphatidylinositol 3-kinase (PtdIns3K) complexes that play a key role in autophagy nucleation and elongation. Here, we show that AMP-activated protein kinase (AMPK) regulates autophagy by phosphorylating BECN1 at Thr388. Phosphorylation of BECN1 is required for autophagy upon glucose withdrawal. BECN1(T388A), a phosphorylation defective mutant, suppresses autophagy through decreasing the interaction between PIK3C3 (phosphatidylinositol 3-kinase catalytic subunit type 3) and ATG14 (autophagy-related 14). The BECN1(T388A) mutant has a higher affinity for BCL2 than its wild-type counterpart; the mutant is more prone to dimer formation. Conversely, a BECN1 phosphorylation mimic mutant, T388D, has stronger binding to PIK3C3 and ATG14, and promotes higher autophagy activity than the wild-type control. These findings uncover a novel mechanism of autophagy regulation.
英文摘要: Macroautophagy/autophagy is a conserved catabolic process that recycles cytoplasmic material during low energy conditions. BECN1/Beclin1 (Beclin 1, autophagy related) is an essential protein for function of the class 3 phosphatidylinositol 3-kinase (PtdIns3K) complexes that play a key role in autophagy nucleation and elongation. Here, we show that AMP-activated protein kinase (AMPK) regulates autophagy by phosphorylating BECN1 at Thr388. Phosphorylation of BECN1 is required for autophagy upon glucose withdrawal. BECN1(T388A), a phosphorylation defective mutant, suppresses autophagy through decreasing the interaction between PIK3C3 (phosphatidylinositol 3-kinase catalytic subunit type 3) and ATG14 (autophagy-related 14). The BECN1(T388A) mutant has a higher affinity for BCL2 than its wild-type counterpart; the mutant is more prone to dimer formation. Conversely, a BECN1 phosphorylation mimic mutant, T388D, has stronger binding to PIK3C3 and ATG14, and promotes higher autophagy activity than the wild-type control. These findings uncover a novel mechanism of autophagy regulation.
刊物名称: AUTOPHAGY
英文刊物名称: AUTOPHAGY
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学科: Cell Biology
英文学科: Cell Biology
影响因子: 8.593
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论文类别: Article
英文论文类别: Article
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