The inositol 5-phosphatase INPP5K participates in the fine control of ER organization.
The inositol 5-phosphatase INPP5K participates in the fine control of ER organization.
复制标题
肌醇5-磷酸酶INPP5K参与ER组织的精细控制。
DOI：
10.1083/jcb.201802125
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发表时间：
2018-10-01
期刊：
影响因子：
--
通讯作者：
De Camilli P
中科院分区：
文献类型：
--
作者：
Dong R;Zhu T;Benedetti L;Gowrishankar S;Deng H;Cai Y;Wang X;Shen K;De Camilli P
Endoplasmic reticulum (ER) morphology is dynamic and key to its function during different cellular processes. Dong et al. now show in convergent studies in human cells and Caenorhabditis elegans neurons that a phosphoinositide phosphatase (INPP5K) is localized on the surface of the ER network and helps control the shape of the ER. INPP5K (SKIP) is an inositol 5-phosphatase that localizes in part to the endoplasmic reticulum (ER). We show that recruitment of INPP5K to the ER is mediated by ARL6IP1, which shares features of ER-shaping proteins. Like ARL6IP1, INPP5K is preferentially localized in ER tubules and enriched, relative to other ER resident proteins (Sec61β, VAPB, and Sac1), in newly formed tubules that grow along microtubule tracks. Depletion of either INPP5K or ARL6IP1 results in the increase of ER sheets. In a convergent but independent study, a screen for mutations affecting the distribution of the ER network in dendrites of the PVD neurons of Caenorhabditis elegans led to the isolation of mutants in CIL-1, which encodes the INPP5K worm orthologue. The mutant phenotype was rescued by expression of wild type, but not of catalytically inactive CIL-1. Our results reveal an unexpected role of an ER localized polyphosphoinositide phosphatase in the fine control of ER network organization.
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DOI：
10.1083/jcb.200911024
发表时间：
2010-08-09
期刊：
The Journal of cell biology
影响因子：
--
作者：
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DOI：
10.1016/j.bbalip.2015.02.013
发表时间：
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期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
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通讯作者：
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影响因子：
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作者：
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