Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 48, Pages E10389-E10398Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1711408114
Keywords
ERES; Sec16; ERGIC; ER stress; GM130
Categories
Funding
- European Molecular Biology Laboratory (EMBL) Advanced Light Microscopy Facility (ALMF)
- Zeiss
- European Molecular Biology Organization
- Deutsche Forschungsgemeinschaft [LE 546/7-1]
- North Rhine-Westphalia Graduate School for Genetics and Functional Genomics
- EMBL Interdisciplinary Postdoctoral Programme under Marie Curie Actions
- EMBL
Ask authors/readers for more resources
Tango1 enables ER-to-Golgi trafficking of large proteins. We show here that loss of Tango1, in addition to disrupting protein secretion and ER/Golgi morphology, causes ER stress and defects in cell shape. We find that the previously observed dependence of smaller cargos on Tango1 is a secondary effect. If large cargos like Dumpy, which we identify as a Tango1 cargo, are removed from the cell, nonbulky proteins reenter the secretory pathway. Removal of blocking cargo also restores cell morphology and attenuates the ER-stress response. Thus, failures in the secretion of nonbulky proteins, ER stress, and defective cell morphology are secondary consequences of bulky cargo retention. By contrast, ER/Golgi defects in Tango1-depleted cells persist in the absence of bulky cargo, showing that they are due to a secretion-independent function of Tango1. Therefore, maintenance of ER/Golgi architecture and bulky cargo transport are the primary functions for Tango1.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available