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SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P

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Horstmann,  Heinz
Synaptic Transmission MNTB, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;
Synaptic Transmission, Max Planck Institute for Medical Research, Max Planck Society;
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Xu, Y., Horstmann, H., Seet, L., Wong, S. H., & Hong, W. (2001). SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nature Cell Biology, 3, 658-666. doi:10.1038/35083051.


Cite as: https://hdl.handle.net/21.11116/0000-0000-3E76-7
Abstract
The sorting nexin (SNX) protein family is implicated in regulating membrane traffic, but the mechanism is still unknown. We show that SNX3 is associated with the early endosome through a novel motif (PX domain) capable of interaction with phosphatidylinositol-3-phosphate (PtdIns(3)P). Overexpression of SNX3 alters endosomal morphology and delays transport to the lysosome. Transport from the early to the recycling endosome is affected upon microinjection of SNX3 antibodies. Our results highlight a novel mechanism by which SNX proteins regulate traffic and uncover a novel class of effectors for PtdIns(3)P.