AMPK phosphorylates GBF1 for mitotic Golgi disassembly
AMPK phosphorylates GBF1 for mitotic Golgi disassembly
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AMPK 磷酸化 GBF1 以促进有丝分裂高尔基体分解
DOI：
10.1242/jcs.121954
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发表时间：
2013-03-15
影响因子：
4
通讯作者：
Liu, Wei
中科院分区：
文献类型：
--
作者：
Mao, Luna;Li, Ning;Liu, Wei
摘要在哺乳动物细胞中，高尔基体在有丝分裂过程中经历了广泛的碎裂；这不仅是复合体分裂所必需的，也是有丝分裂过程所必需的。然而，高尔基体有丝分裂碎裂的分子机制还远不清楚。在这里，我们展示了AMP激活的蛋白激酶(AMPK)被磷酸化，并在细胞进入有丝分裂时被激活。活化的AMPK使GBF1磷酸化，GBF1是Arf-GTP酶的一种鸟嘌呤核苷酸交换因子，使GBF1与高尔基体膜解离，并取消GBF1作为Arf1-GTP酶的作用。我们进一步证明，AMPK和GBF1的磷酸化对于高尔基体的分解和随后的有丝分裂进入是必不可少的。这些数据表明，AMPK-GBF1-Arf1信号参与了有丝分裂过程中高尔基体碎裂的调节。
Summary In mammalian cells, the Golgi apparatus undergoes extensive fragmentation during mitosis; this is required not only for the partitioning of the complex but also for the process of mitosis. However, the molecular mechanism underlying the mitotic fragmentation of the Golgi is far from clear. Here, we show that AMP-activated protein kinase (AMPK) is phosphorylated and activated when cells enter mitosis. Activated AMPK phosphorylates GBF1, a guanine nucleotide exchange factor (GEF) for Arf-GTPases, disassociating GBF1 from the Golgi membrane and abolishing the action of GBF1 as an Arf1-GEF. We further demonstrate that the phosphorylation of AMPK and GBF1 is essential for Golgi disassembly and subsequent mitosis entry. These data suggest that AMPK–GBF1–Arf1 signaling is involved in the regulation of Golgi fragmentation during mitosis.