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

STX19 is an unusual Q -SNARE as it lacks a C-terminal transmembrane domain. However, it is efficiently targeted to post-Golgi membranes. Here, we set out to determine the intracellular localisation of endogenous STX19 and elucidate the mechanism by which it is targeted to membranes. We have found th...

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Veröffentlicht in:Journal of cell science 2018-10, Vol.131 (20)
Hauptverfasser: Ampah, Khamal K, Greaves, Jennifer, Shun-Shion, Amber S, Asnawi, Asral W, Lidster, Jessica A, Chamberlain, Luke H, Collins, Mark O, Peden, Andrew A
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container_end_page
container_issue 20
container_start_page
container_title Journal of cell science
container_volume 131
creator Ampah, Khamal K
Greaves, Jennifer
Shun-Shion, Amber S
Asnawi, Asral W
Lidster, Jessica A
Chamberlain, Luke H
Collins, Mark O
Peden, Andrew A
description STX19 is an unusual Q -SNARE as it lacks a C-terminal transmembrane domain. However, it is efficiently targeted to post-Golgi membranes. Here, we 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 colocalises with MICAL-L1 and Rab8 (which has Rab8a and Rab8b forms). 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 a 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.This article has an associated First Person interview with the first author of the paper.
doi_str_mv 10.1242/jcs.212498
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subjects Acylation - genetics
Humans
Protein Transport - genetics
Q-SNARE Proteins - metabolism
title S-acylation regulates the trafficking and stability of the unconventional Q-SNARE STX19
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