TRAPPC13 Modulates Autophagy and the Response to Golgi Stress

Overview

Journal J Cell Sci

Specialty Cell Biology

Date 2017 May 25

PMID 28536105

Citations 22

Authors

Silvia Ramirez-Peinado

Tatiana I Ignashkova

Bram J van Raam

Jan Baumann

Erica L Sennott

Mathieu Gendarme

Ralph K Lindemann

Michael N Starnbach

Jan H Reiling

Affiliations

Soon will be listed here.

Abstract

Tether complexes play important roles in endocytic and exocytic trafficking of lipids and proteins. In yeast, the multisubunit transport protein particle (TRAPP) tether regulates endoplasmic reticulum (ER)-to-Golgi and intra-Golgi transport and is also implicated in autophagy. In addition, the TRAPP complex acts as a guanine nucleotide exchange factor (GEF) for Ypt1, which is homologous to human Rab1a and Rab1b. Here, we show that human TRAPPC13 and other TRAPP subunits are critically involved in the survival response to several Golgi-disrupting agents. Loss of TRAPPC13 partially preserves the secretory pathway and viability in response to brefeldin A, in a manner that is dependent on ARF1 and the large GEF GBF1, and concomitant with reduced caspase activation and ER stress marker induction. TRAPPC13 depletion reduces Rab1a and Rab1b activity, impairs autophagy and leads to increased infectivity to the pathogenic bacterium in response to brefeldin A. Thus, our results lend support for the existence of a mammalian TRAPPIII complex containing TRAPPC13, which is important for autophagic flux under certain stress conditions.

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