Yu Cao
@caolab.bsky.social
Professor at Shanghai Jiao Tong University School of Medicine.
Structural Biology, Cell homeostasis, Membrane protein
Structural Biology, Cell homeostasis, Membrane protein
How does the ER send misfolded proteins to destruction?
Our new Communications Biology study uncovers a 6:6 Derlin-1/p97 complex, a dynamic channel that bridges ER quality control with cytoplasmic degradation.
rdcu.be/eLMSx
Our new Communications Biology study uncovers a 6:6 Derlin-1/p97 complex, a dynamic channel that bridges ER quality control with cytoplasmic degradation.
rdcu.be/eLMSx
October 20, 2025 at 1:06 AM
How does the ER send misfolded proteins to destruction?
Our new Communications Biology study uncovers a 6:6 Derlin-1/p97 complex, a dynamic channel that bridges ER quality control with cytoplasmic degradation.
rdcu.be/eLMSx
Our new Communications Biology study uncovers a 6:6 Derlin-1/p97 complex, a dynamic channel that bridges ER quality control with cytoplasmic degradation.
rdcu.be/eLMSx
Our latest cryo-EM study reveals the architecture of the KOGG complex, a key player in collagen lysine O-link glycosylation. This LH3/ColGalT1 enzyme machinery ensures proper collagen maturation and may even form fiber-like supercomplexes! #Glycosylation #Collagen
doi.org/10.1038/s41467-025-57768-9
doi.org/10.1038/s41467-025-57768-9
The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation - Nature Communications
This study reveals the structural basis of collagen processing by the KOGG complex, revealing how it catalyzes lysine hydroxylation and dual-glycosylation, essential for collagen folding and stability...
www.nature.com
March 15, 2025 at 4:47 AM
Our latest cryo-EM study reveals the architecture of the KOGG complex, a key player in collagen lysine O-link glycosylation. This LH3/ColGalT1 enzyme machinery ensures proper collagen maturation and may even form fiber-like supercomplexes! #Glycosylation #Collagen
doi.org/10.1038/s41467-025-57768-9
doi.org/10.1038/s41467-025-57768-9