Journal
TOXINS
Volume 13, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/toxins13080543
Keywords
cholera toxin B-subunit; membrane nanodomains; endocytosis; retrograde trafficking; membrane curvature; membrane rafts; glycolipids; GM1; GL-Lect hypothesis
Categories
Funding
- National Science Foundation [DMR-1652316]
- National Institutes of Health [R37 DK048106, RO1 DK104868, P30 DK034854, R01 GM106720]
- Harrington Scholar Innovator Award
- Harvard Digestive Diseases Center
Ask authors/readers for more resources
CTxB is a stable homopentameric protein that tightly binds up to five GM1 glycosphingolipids, providing an important tool for studying membrane structure and dynamics.
Cholera toxin B-subunit (CTxB) has emerged as one of the most widely utilized tools in membrane biology and biophysics. CTxB is a homopentameric stable protein that binds tightly to up to five GM1 glycosphingolipids. This provides a robust and tractable model for exploring membrane structure and its dynamics including vesicular trafficking and nanodomain assembly. Here, we review important advances in these fields enabled by use of CTxB and its lipid receptor GM1.
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
Share Paper
