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The inositol 5-phosphatase INPP5K participates in the fine control of ER organization.

The Journal of cell biology | 2018

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.

Pubmed ID: 30087126 RIS Download

Research resources used in this publication

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Associated grants

  • Agency: NIDA NIH HHS, United States
    Id: P30 DA018343
  • Agency: NIDDK NIH HHS, United States
    Id: P30 DK045735
  • Agency: NINDS NIH HHS, United States
    Id: R01 NS036251
  • Agency: Howard Hughes Medical Institute, United States

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