biostudies-literatureSun RPurdue Center for Cancer ResearchSusan G. Komen Breast Cancer FoundationPurdue Institute for Drug Discovery (PIDD) Programmatic Area grantRalph W. and Grace M. Showalter Research Trust grantNIGMS NIH HHS162https://www.ebi.ac.uk/biostudies/studies/S-EPMC8750214biostudies-literatureUnknown11(1)Leveraging the T cell immunity against tumors represents a revolutionary type of cancer therapy. 4-1BB is a well-characterized costimulatory immune receptor existing on activated T cells and mediating their proliferation and cytotoxicity under infectious diseases and cancers. Despite the accumulating interest in implementing 4-1BB as a therapeutic target for immune-related disorders, less is known about the pattern of its intracellular behaviors and regulations. It has been previously demonstrated that 4-1BB is heavily modified by <i>N</i>-glycosylation; however, the biological importance of this modification lacks detailed elucidation. Through biochemical, biophysical, and cell-biological approaches, we systematically evaluated the impact of <i>N</i>-glycosylation on the ligand interactioCells<i>N</i>-Glycosylation Facilitates 4-1BB Membrane Localization by Avoiding Its Multimerization.PMC8750214N/AR24 GM137782CCR17488088Kim AMJSun RLim SOMurray AAfalse<i>N</i>-Glycosylation Facilitates 4-1BB Membrane Localization by Avoiding Its Multimerization.Leveraging the T cell immunity against tumors represents a revolutionary type of cancer therapy. 4-1BB is a well-characterized costimulatory immune receptor existing on activated T cells and mediating their proliferation and cytotoxicity under infectious diseases and cancers. Despite the accumulating interest in implementing 4-1BB as a therapeutic target for immune-related disorders, less is known about the pattern of its intracellular behaviors and regulations. It has been previously demonstrated that 4-1BB is heavily modified by <i>N</i>-glycosylation; however, the biological importance of this modification lacks detailed elucidation. Through biochemical, biophysical, and cell-biological approaches, we systematically evaluated the impact of <i>N</i>-glycosylation on the ligand interactio2022-01-01T00:00:00Z2022 Jan2026-04-08T06:49:28.557Z2022-02-11T16:16:58.905ZS-EPMC87502143501172410.3390/cells11010162