Unknown

Dataset Information

0

IPIP27 Coordinates PtdIns(4,5)P2 Homeostasis for Successful Cytokinesis.

ABSTRACT: During cytokinesis, an actomyosin contractile ring drives the separation of the two daughter cells. A key molecule in this process is the inositol lipid PtdIns(4,5)P2, which recruits numerous factors to the equatorial region for contractile ring assembly. Despite the importance of PtdIns(4,5)P2 in cytokinesis, the regulation of this lipid in cell division remains poorly understood. Here, we identify a role for IPIP27 in mediating cellular PtdIns(4,5)P2 homeostasis. IPIP27 scaffolds the inositol phosphatase oculocerebrorenal syndrome of Lowe (OCRL) by coupling it to endocytic BAR domain proteins. Loss of IPIP27 causes accumulation of PtdIns(4,5)P2 on aberrant endomembrane vacuoles, mislocalization of the cytokinetic machinery, and extensive cortical membrane blebbing. This phenotype is observed in Drosophila and human cells and can result in cytokinesis failure. We have therefore identified IPIP27 as a key modulator of cellular PtdIns(4,5)P2 homeostasis required for normal cytokinesis. The results indicate that scaffolding of inositol phosphatase activity is critical for maintaining PtdIns(4,5)P2 homeostasis and highlight a critical role for this process in cell division.

SUBMITTER: Carim SC 

PROVIDER: S-EPMC6408333 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

IPIP27 Coordinates PtdIns(4,5)P<sub>2</sub> Homeostasis for Successful Cytokinesis.

Carim Sabrya C SC   Ben El Kadhi Khaled K   Yan Guanhua G   Sweeney Sean T ST   Hickson Gilles R GR   Carréno Sébastien S   Lowe Martin M  

Current biology : CB 20190221 5

During cytokinesis, an actomyosin contractile ring drives the separation of the two daughter cells. A key molecule in this process is the inositol lipid PtdIns(4,5)P<sub>2</sub>, which recruits numerous factors to the equatorial region for contractile ring assembly. Despite the importance of PtdIns(4,5)P<sub>2</sub> in cytokinesis, the regulation of this lipid in cell division remains poorly understood. Here, we identify a role for IPIP27 in mediating cellular PtdIns(4,5)P<sub>2</sub> homeostasi  ...[more]

Similar Datasets

Unknown Decrease in plasma membrane tension triggers PtdIns(4,5)P<sub>2</sub> phase separation to inactivate TORC2.
| S-EPMC6237274 | biostudies-literature
Unknown The NOXO1β PX domain preferentially targets PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
| S-EPMC3304020 | biostudies-literature
Unknown PtdIns(4,5)P<sub>2</sub> stabilizes active states of GPCRs and enhances selectivity of G-protein coupling.
| S-EPMC6059376 | biostudies-literature
Unknown FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P<sub>2</sub>-dependent switch.
| S-EPMC9054013 | biostudies-literature
Unknown COMMD1 and PtdIns(4,5)P<sub>2</sub> interaction maintain ATP7B copper transporter trafficking fidelity in HepG2 cells.
| S-EPMC6803360 | biostudies-literature
Unknown Regulating angiogenesis at the level of PtdIns-4,5-P2.
| S-EPMC1462986 | biostudies-literature
Unknown RDGB?, a PtdIns-PtdOH transfer protein, regulates G-protein-coupled PtdIns(4,5)P2 signalling during Drosophila phototransduction.
| S-EPMC4582195 | biostudies-literature
Unknown Hippocampal neurons maintain a large PtdIns(4)P pool that results in faster PtdIns(4,5)P2 synthesis.
| S-EPMC8906353 | biostudies-literature
Unknown The phox domain of sorting nexin 5 lacks phosphatidylinositol 3-phosphate (PtdIns(3)P) specificity and preferentially binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
| S-EPMC2749144 | biostudies-literature
Unknown ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P <sub>2</sub>) and regulate its level at the plasma membrane.
| S-EPMC5624964 | biostudies-literature