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© Research
Publication : The Journal of cell biology

PTEN reduces endosomal PtdIns(4,5)P in a phosphatase-independent manner via a PLC pathway

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of cell biology - 22 May 2019

Mondin VE, Ben El Kadhi K, Cauvin C, Jackson-Crawford A, Bélanger E, Decelle B, Salomon R, Lowe M, Echard A, Carréno S

Link to Pubmed [PMID] – 31118240

J. Cell Biol. 2019 Jul;218(7):2198-2214

The tumor suppressor PTEN dephosphorylates PtdIns(3,4,5)P into PtdIns(4,5)P Here, we make the unexpected discovery that in PTEN reduces PtdIns(4,5)P levels on endosomes, independently of its phosphatase activity. This new PTEN function requires the enzymatic action of dPLCXD, an atypical phospholipase C. Importantly, we discovered that this novel PTEN/dPLCXD pathway can compensate for depletion of dOCRL, a PtdIns(4,5)P phosphatase. Mutation of OCRL1, the human orthologue of dOCRL, causes oculocerebrorenal Lowe syndrome, a rare multisystemic genetic disease. Both OCRL1 and dOCRL loss have been shown to promote accumulation of PtdIns(4,5)P on endosomes and cytokinesis defects. Here, we show that PTEN or dPLCXD overexpression prevents these defects. In addition, we found that chemical activation of this pathway restores normal cytokinesis in human Lowe syndrome cells and rescues OCRL phenotypes in a zebrafish Lowe syndrome model. Our findings identify a novel PTEN/dPLCXD pathway that controls PtdIns(4,5)P levels on endosomes. They also point to a potential new strategy for the treatment of Lowe syndrome.

https://www.ncbi.nlm.nih.gov/pubmed/31118240