SNX18 shares a redundant role with SNX9 and modulates endocytic trafficking at the plasma membrane

Joohyun Park, Yoonju Kim, Suho Lee, Jae Jun Park, Zee Yong Park, Woong Sun, Hyun Kim, Sunghoe Chang

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

SNX18 and SNX9 are members of a subfamily of SNX (sorting nexin) proteins with the same domain structure. Although a recent report showed that SNX18 and SNX9 localize differently in cells and appear to function in different trafficking pathways, concrete evidence regarding whether they act together or separately in intracellular trafficking is still lacking. Here, we show that SNX18 has a similar role to SNX9 in endocytic trafficking at the plasma membrane, rather than having a distinct role. SNX18 and SNX9 are expressed together in most cell lines, but to a different extent. Like SNX9, SNX18 interacts with dynamin and stimulates the basal GTPase activity of dynamin. It also interacts with neuronal Wiskott-Aldrich syndrome protein (N-WASP) and synaptojanin, as does SNX9. SNX18 and SNX9 can form a heterodimer and colocalize in tubular membrane structures. Depletion of SNX18 by small hairpin RNA inhibited transferrin uptake. SNX18 successfully compensates for SNX9 deficiency during clathrin-mediated endocytosis and vice versa. Total internal reflection fluorescence microscopy in living cells shows that a transient burst of SNX18 recruitment to clathrin-coated pits coincides spatiotemporally with a burst of dynamin and SNX9. Taken together, our results suggest that SNX18 functions with SNX9 in multiple pathways of endocytosis at the plasma membrane and that they are functionally redundant.

Original languageEnglish
Pages (from-to)1742-1750
Number of pages9
JournalJournal of Cell Science
Volume123
Issue number10
DOIs
Publication statusPublished - 2010 May 15

Keywords

  • Clathrin-mediated endocytosis
  • Dynamin
  • Membrane tubulation
  • SNX18
  • SNX9

ASJC Scopus subject areas

  • Cell Biology

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