Journal
CELL REPORTS
Volume 6, Issue 5, Pages 878-891Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2014.01.040
Keywords
-
Categories
Funding
- Howard Hughes Medical Institute International Student Research Fellowship
- NRSA [1-F32-AI098384]
- NIH [NIAID 5T32AI007520]
- National Institutes of Health [NIAID RO1AI083359, NIGMS R01GM100486]
- Welch Foundation [I-1704]
- Burroughs Wellcome Fund
Ask authors/readers for more resources
Bidirectional vesicular transport between the endoplasmic reticulum (ER) and Golgi is mediated largely by ARF and Rab GTPases, which orchestrate vesicle fission and fusion, respectively. How their activities are coordinated in order to define the successive steps of the secretory pathway and preserve traffic directionality is not well understood in part due to the scarcity of molecular tools that simultaneously target ARF and Rab signaling. Here, we take advantage of the unique scaffolding properties of E. coli secreted protein G (EspG) to describe the critical role of ARF1/Rab1 spatiotemporal coordination in vesicular transport at the ER-Golgi intermediate compartment. Structural modeling and cellular studies show that EspG induces bidirectional traffic arrest by tethering vesicles through select ARF1-GTP/effector complexes and local inactivation of Rab1. The mechanistic insights presented here establish the effectiveness of a small bacterial catalytic scaffold for studying complex processes and reveal an alternative mechanism of immune regulation by an important human pathogen.
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