S-acylation regulates the trafficking and stability of the unconventional Q-SNARE STX19

Khamal K. Ampah, Jennifer Greaves, Amber S. M. Shun-Shion, Asral W. B. A. Asnawi, Jessica A. Lidster, Luke H. Chamberlain, Mark O. Collins, Andrew A. Peden

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)
50 Downloads (Pure)


STX19 is an unusual Qa-SNARE as it lacks a C-terminal transmembrane domain. However, it is efficiently targeted to post-Golgi membranes. We have set out to determine the intracellular localisation of endogenous STX19 and elucidate the mechanism by which it is targeted to membranes. We have found that a pool of STX19 is localised to tubular recycling endosomes where it co-localises with MICAL-L1 and Rab8. Using a combination of genetic, biochemical and cell based approaches we have identified that STX19 is S-acylated at its C-terminus and is a substrate for several Golgi localised S-acyltransferases, suggesting that STX19 is initially S-acylated at the Golgi before trafficking to the plasma membrane and endosomes. Surprisingly, we have found that S-acylation is the key determinant in targeting STX19 to tubular recycling endosomes, suggesting that S-acylation may play a general role in directing proteins to this compartment. In addition, S-acylation also protects STX19 from proteosomal degradation indicating that S-acylation regulates the function of STX19 at multiple levels.
Original languageEnglish
Number of pages48
JournalJournal of Cell Science
Early online date25 Sept 2018
Publication statusE-pub ahead of print - 25 Sept 2018


  • S-acylation
  • palmitoylation
  • STX19
  • MICAL-L1
  • Rab8


Dive into the research topics of 'S-acylation regulates the trafficking and stability of the unconventional Q-SNARE STX19'. Together they form a unique fingerprint.

Cite this