LAG3 facilitates MHC Ⅱ trogocytosis with assistance of the ER-PM junction

Additional information

The online version contains supplementary materials available at http://www.jbr-pub.org.cn/article/doi/10.7555/JBR.39.20250144.

References

[1] Aggarwal V, Workman CJ, Vignali DAA. LAG-3 as the third checkpoint inhibitor[J]. Nat Immunol, 2023, 24(9): 1415-1422. doi: 10.1038/s41590-023-01569-z

[2] Maruhashi T, Sugiura D, Okazaki IM, et al. Binding of LAG-3 to stable peptide-MHC class Ⅱ limits T cell function and suppresses autoimmunity and anti-cancer immunity[J]. Immunity, 2022, 55(5): 912-924.e8.

[3] Jiang Y, Dai A, Huang Y, et al. Ligand-induced ubiquitination unleashes LAG3 immune checkpoint function by hindering membrane sequestration of signaling motifs[J]. Cell, 2025, 188(9): 2354-2371.e18.

[4] Guy C, Mitrea DM, Chou PC, et al. LAG3 associates with TCR-CD3 complexes and suppresses signaling by driving co-receptor-Lck dissociation[J]. Nat Immunol, 2022, 23(5): 757-767. doi: 10.1038/s41590-022-01176-4

[5] Ming Q, Celias DP, Wu C, et al. LAG3 ectodomain structure reveals functional interfaces for ligand and antibody recognition[J]. Nat Immunol, 2022, 23(7): 1031-1041. doi: 10.1038/s41590-022-01238-7

[6] Ming Q, Antfolk D, Price DA, et al. Structural basis for mouse LAG3 interactions with the MHC class Ⅱ molecule I-A^b[J]. Nat Commun, 2024, 15(1): 7513. doi: 10.1038/s41467-024-51930-5

[7] Petersen J, Llerena C, Golzarroshan B, et al. Crystal structure of the human LAG-3-HLA-DR1-peptide complex[J]. Sci Immunol, 2024, 9(102): eads5122. doi: 10.1126/sciimmunol.ads5122

[8] Xu F, Du W, Zou Q, et al. COPII mitigates ER stress by promoting formation of ER whorls[J]. Cell Res, 2021, 31(2): 141-156. doi: 10.1038/s41422-020-00416-2

[9] Prinz WA, Toulmay A, Balla T. The functional universe of membrane contact sites[J]. Nat Rev Mol Cell Biol, 2020, 21(1): 7-24. doi: 10.1038/s41580-019-0180-9

[10] Wakamatsu E, Machiyama H, Toyota H, et al. Indirect suppression of CD4 T cell activation through LAG-3-mediated trans-endocytosis of MHC class Ⅱ[J]. Cell Rep, 2024, 43(9): 114655. doi: 10.1016/j.celrep.2024.114655

[11] Joly E, Hudrisier D. What is trogocytosis and what is its purpose?[J]. Nat Immunol, 2003, 4(9): 815. doi: 10.1038/ni0903-815

[12] Qureshi OS, Zheng Y, Nakamura K, et al. Trans-endocytosis of CD80 and CD86: A molecular basis for the cell-extrinsic function of CTLA-4[J]. Science, 2011, 332(6029): 600-603. doi: 10.1126/science.1202947

[13] Gary R, Voelkl S, Palmisano R, et al. Antigen-specific transfer of functional programmed death ligand 1 from human APCs onto CD8⁺ T cells via trogocytosis[J]. J Immunol, 2012, 188(2): 744-752. doi: 10.4049/jimmunol.1101412

[14] Caldieri G, Barbieri E, Nappo G, et al. Reticulon 3-dependent ER-PM contact sites control EGFR nonclathrin endocytosis[J]. Science, 2017, 356(6338): 617-624. doi: 10.1126/science.aah6152

[15] Stinchcombe JC, Asano Y, Kaufman CJG, et al. Ectocytosis renders T cell receptor signaling self-limiting at the immune synapse[J]. Science, 2023, 380(6647): 818-823. doi: 10.1126/science.abp8933

[16] Wu H, Carvalho P, Voeltz GK. Here, there, and everywhere: The importance of ER membrane contact sites[J]. Science, 2018, 361(6401): 466. doi: 10.1126/science.aan5835

[17] Luik RM, Wang B, Prakriya M, et al. Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation[J]. Nature, 2008, 454(7203): 538-542. doi: 10.1038/nature07065

[18] Jamecna D, Antonny B. Intrinsically disordered protein regions at membrane contact sites[J]. Biochim Biophys Acta Mol Cell Biol Lipids, 2021, 1866(11): 159020. doi: 10.1016/j.bbalip.2021.159020