p97/p47-Mediated biogenesis of Golgi and ER.
p97/p47-Mediated biogenesis of Golgi and ER.
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DOI：
10.1093/jb/mvi028
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发表时间：
2005-02
影响因子：
2.7
通讯作者：
K. Uchiyama;Hisao Kondo
中科院分区：
文献类型：
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作者：
K. Uchiyama;Hisao Kondo
在哺乳动物细胞中，高尔基体和内质网在间期具有典型的结构：位于细胞核附近的堆叠池和遍布细胞质的相互连接的小管网络。在有丝分裂时，它们的结构消失并重新组装成子细胞。p97是一种AAA-ATP酶，介导膜融合，并且是这些细胞器重新组装所必需的。在p97介导的膜融合中，p47被鉴定为必需的辅因子，通过其p97结合到SNARE，突触融合蛋白5。第二个必需的辅因子，VCIP 135，被确定为p97/p47/syntaxin 5相互作用蛋白。最近的一些证据表明，泛素化可能涉及p97/p47途径; p47结合到monoubiquitinated蛋白质和VCIP 135显示出体外去泛素化活性。对于p97/p47通路的细胞周期调控，已经报道p47的定位和磷酸化-去磷酸化是至关重要的。在这篇综述中，我们描述了参与p97介导的膜融合的组件，并讨论了融合途径的调节。
In mammalian cells, the Golgi apparatus and endoplasmic reticulum have typical structures during interphase: stacked cisternae located adjacent to the nucleus and a network of interconnected tubules throughout the cytoplasm, respectively. At mitosis their architectures disappear and are reassembled in daughter cells. p97, an AAA-ATPase, mediates membrane fusion and is required for reassembly of these organelles. In the p97-mediated membrane fusion, p47 was identified as an essential cofactor, through which p97 binds to a SNARE, syntaxin5. A second essential cofactor, VCIP135, was identified as a p97/p47/syntaxin5-interacting protein. Several lines of recent evidence suggest that ubiquitination may be implicated in the p97/p47 pathway; p47 binds to monoubiquitinated proteins and VCIP135 shows a deubiquitinating activity in vitro. For the cell-cycle regulation of the p97/p47 pathway, it has been reported that the localization and phosphorylation-dephosphorylation of p47 are crucial. In this review, we describe the components involved in the p97-mediated membrane fusion and discuss the regulation of the fusion pathway.