Article abstract
Nature Cell Biology 3, 658 - 666 (2001)
Published online: 8 June 2001 | doi:10.1038/35083051
SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P
Yue Xu1, Heinz Hortsman1, Lifong Seet1, Siew Heng Wong1 & Wanjin Hong1
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.
- Membrane Biology Laboratory, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117609, Singapore
Correspondence to: Wanjin Hong1 e-mail: mcbhwj@imcb.nus.edu.sg
