PD-L1(CD274) glycosylation and translocation to plasma membrane

Summary
Organism
Homo sapiens (human)
Reactome
R-HSA-9931295
PubChem
R-HSA-9931295
Description
  • PD-L1 (CD274) glycosylation plays a critical role in determining the protein function and stability. PD-L1 is N-glycosylated at N192, N200 and N219 by the OST complex in the ER lumen. This process is important for PD-L1 stability and inhibits its targeting for proteasomal degradation by GSK3B (Li et al., 2016). Also, JAK1 activated by IL6 pathway positively regulates the glycosylation process by aiding in the process of recruiting endoplasmic reticulum-associated N-glycosyltransferase STT3A (part of the OST complex) to catalyse PD-L1 glycosylation (Chan et al., 2019). PD-L1 is phosphorylated by IL6-activated JAK1 at Tyr112 (Y112). This process aids in stabilizing the PD-L1 protein. PD-L1, once glycosylated in the ER lumen, get translocated to the Golgi complex for further glycosylation by B3GNT3 (Li et al., 2018) and K63-ubiquitination by MIB2 (Yu et al., 2023). Post Golgi, PD-L1 gets transported to the plasma membrane where it can bind with its receptor and induce immune tolerance.
Click on a node on the pathway to see its details. Glycoproteins are marked with a glycoprotein icon in their name.

About Release Notes Help Feedback

Click here to visit the beta site.


International Collaboration

GlyCosmos is a member of the GlySpace Alliance together with GlyGen and Glycomics@ExPASy.

Acknowledgements

Supported by JST NBDC Grant Number JPMJND2204

Partly supported by NIH Common Fund Grant #1U01GM125267-01


Logo License Policies Site Map

Contact: [email protected]

This work is licensed under Creative Commons Attribution 4.0 International


GlyCosmos Portal v4.5.0

Last updated: April 6, 2026