Palmitoylated ras proteins traffic through recycling endosomes to the plasma membrane during exocytosis

Ryo Misaki, Miki Morimatsu, Takefumi Uemura, Satoshi Waguri, Eiji Miyoshi, Naoyuki Taniguchi, Michiyuki Matsuda, Tomohiko Taguchi

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)

Abstract

Ras proteins regulate cell growth, death, and differentiation, and it is well established that this functional versatility is accomplished through their different subcellular localizations. Palmitoylated H- and N-Ras are believed to localize at the perinuclear Golgi and plasma membrane (PM). Notably, however, recycling endosomes (REs) also localize to a perinuclear region, which is often indistinguishable from the Golgi. In this study, we show that active palmitoylated Ras proteins mainly localize intracellularly at REs and that REs act as a way station along the post-Golgi exocytic pathway to the PM. H-Ras requires two palmitoyl groups for RE targeting. The lack of either or both palmitoyl groups leads to the mislocalization of the mutant proteins to the endoplasmic reticulum, Golgi apparatus, or the PM. Therefore, we demonstrate that palmitoylation directs Ras proteins to the correct intracellular organelles for trafficking and activity.

Original languageEnglish
Pages (from-to)23-29
Number of pages7
JournalJournal of Cell Biology
Volume191
Issue number1
DOIs
Publication statusPublished - 2010 Oct 4

ASJC Scopus subject areas

  • Cell Biology

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