Journal
CELL REPORTS
Volume 20, Issue 10, Pages 2287-2293Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2017.08.035
Keywords
-
Categories
Funding
- NIH [R01 GM086487, GM078450, GM109863, GM099943]
- NIH Chemistry and Biology Interface training grant [T32 GM008720]
Ask authors/readers for more resources
The Get1/2 transmembrane complex drives the insertion of tail-anchored ( TA) proteins from the cytosolic chaperone Get3 into the endoplasmic reticulum membrane. Mechanistic insight into how Get1/2 coordinates this process is confounded by a lack of understanding of the basic architecture of the complex. Here, we define the oligomeric state of full-length Get1/2 in reconstituted lipid bilayers by combining single-molecule and bulk fluorescence measurements with quantitative in vitro insertion analysis. We show that a single Get1/2 heterodimer is sufficient for insertion and demonstrate that the conserved cytosolic regions of Get1 and Get2 bind asymmetrically to opposing subunits of the Get3 homodimer. Altogether, our results define a simplified model for how Get1/2 and Get3 coordinate TA protein insertion.
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