Rab10 GTPase regulates ER dynamics and morphology.

Rab10 GTPase regulates ER dynamics and morphology.
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DOI:
10.1038/ncb2647
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发表时间:
2013-02
影响因子:
21.3
通讯作者:
--
中科院分区:
生物学1区
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我们已经确定Rab10是内质网特异性的Rab GTPase,它调节内质网结构和动力学。我们发现Rab10定位于内质网和动态内质网相关结构,这些结构沿着微管跟踪并标记新的内质网小管生长的位置。Rab10缺失或Rab10 gdp锁定突变体的表达会改变内质网形态,导致内质网小管减少。我们证明这种缺陷是由于动态内质网小管生长和成功融合邻近内质网的能力降低。与这一功能一致的是,Rab10在几乎一半的内质网小管动态的前缘发现了动态内质网相关结构域。有趣的是,这个Rab10结构域富含至少两种调节磷脂合成的内质网酶,PI合成酶和CEPT1。这个Rab10/PIS/CEPT1动态结构域的形成和功能都被一个gdp锁定的Rab10突变体的表达所抑制。总之,这些数据表明Rab10调节内质网动力学,并进一步表明这些动力学可能与磷脂合成耦合。
We have identified Rab10 as an ER specific Rab GTPase that regulates ER structure and dynamics. We show that Rab10 localizes to the ER and to dynamic ER-associated structures that track along microtubules and mark the position of new ER tubule growth. Rab10 depletion or expression of a Rab10 GDP-locked mutant alters ER morphology, resulting in decreased ER tubules. We demonstrate that this defect is due to a reduced ability of dynamic ER tubules to grow out and successfully fuse with adjacent ER. Consistent with this function, Rab10 partitions to dynamic ER-associated domains found at the leading edge of almost half of all ER tubule dynamics. Interestingly, this Rab10 domain is highly enriched with at least two ER enzymes that regulate phospholipid synthesis, PI Synthase and CEPT1. Both the formation and function of this Rab10/PIS/CEPT1 dynamic domain is inhibited by expression of a GDP-locked Rab10 mutant. Together, these data demonstrate that Rab10 regulates ER dynamics and further suggests that these dynamics could be coupled to phospholipid synthesis.
DOI: 10.1083/jcb.200911024
发表时间: 2010-08-09
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影响因子: --
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发表时间: 1986-10
期刊: The Journal of cell biology
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