Mayle, K. M., Le, A. M. & Kamei, D. T. The intracellular trafficking pathway of transferrin. Biochim. Biophys. Acta 1820, 264–281 (2012).
Cheng, Y., Zak, O., Aisen, P., Harrison, S. C. & Walz, T. Structure of the human transferrin receptor-transferrin complex. Cell 116, 565–576 (2004).
Candelaria, P. V., Leoh, L. S., Penichet, M. L. & Daniels-Wells, T. R. Antibodies targeting the Transferrin Receptor 1 (TfR1) as direct anti-cancer agents. Front. Immunol. 12, 607692 (2021).
Iacopetta, B. J. & Morgan, E. H. The kinetics of transferrin endocytosis and iron uptake from transferrin in rabbit reticulocytes. J. Biol. Chem. 258, 9108–9115 (1983).
Ciechanover, A., Schwartz, A. L., Dautry-Varsat, A. & Lodish, H. F. Kinetics of internalization and recycling of transferrin and the transferrin receptor in a human hepatoma cell line. Effect of lysosomotropic agents. J. Biol. Chem. 258, 9681–9689 (1983).
Rhee, K. & Zhou, X. Two in one: the emerging concept of bifunctional antibodies. Curr. Opin. Biotechnol. 85, 103050 (2024).
Wells, J. A. & Kumru, K. Extracellular targeted protein degradation: an emerging modality for drug discovery. Nat. Rev. Drug Discov. 23, 126–140 (2024).
Cotton, A. D., Nguyen, D. P., Gramespacher, J. A., Seiple, I. B. & Wells, J. A. Development of antibody-based PROTACs for the degradation of the cell-surface immune checkpoint protein PD-L1. J. Am. Chem. Soc. 143, 593–598 (2021).
Marei, H. et al. Antibody targeting of E3 ubiquitin ligases for receptor degradation. Nature https://doi.org/10.1038/s41586-022-05235-6 (2022).
Gramespacher, J. A., Cotton, A. D., Burroughs, P. W. W., Seiple, I. B. & Wells, J. A. Roadmap for optimizing and broadening antibody-based PROTACs for degradation of cell surface proteins. ACS Chem. Biol. 17, 1259–1268 (2022).
Siepe, D. H., Picton, L. K. & Garcia, K. C. Receptor elimination by E3 ubiquitin ligase recruitment (REULR): a targeted protein degradation toolbox. ACS Synth. Bio. 12, 1081–1093 (2023).
Ahn, G. et al. LYTACs that engage the asialoglycoprotein receptor for targeted protein degradation. Nat. Chem. Biol. 17, 937–946 (2021).
Banik, S. M. et al. Lysosome-targeting chimaeras for degradation of extracellular proteins. Nature 584, 291–297 (2020).
Pance, K. et al. Modular cytokine receptor-targeting chimeras for targeted degradation of cell surface and extracellular proteins. Nat. Biotechnol. https://doi.org/10.1038/s41587-022-01456-2 (2022).
Zhou, Y., Teng, P., Montgomery, N. T., Li, X. & Tang, W. Development of triantennary N-acetylgalactosamine conjugates as degraders for extracellular proteins. ACS Cent Sci 7, 499–506 (2021).
Caianiello, D. F. et al. Bifunctional small molecules that mediate the degradation of extracellular proteins. Nat. Chem. Biol. 17, 947–953 (2021).
Zheng, J. et al. Bifunctional compounds as molecular degraders for integrin-facilitated targeted protein degradation. J. Am. Chem. Soc. 144, 21831–21836 (2022).
Miao, Y. et al. Bispecific aptamer chimeras enable targeted protein degradation on cell membranes. Angew. Chem. Int. Ed. 60, 11267–11271 (2021).
Ahn, G. et al. Elucidating the cellular determinants of targeted membrane protein degradation by lysosome-targeting chimeras. Science 382, eadf6249 (2023).
Shen, F. & Dassama, L. M. K. Opportunities and challenges of protein-based targeted protein degradation. Chem. Sci. 14, 8433–8447 (2023).
Kawabata, H. Transferrin and transferrin receptors update. Free Radic. Biol. Med. 133, 46–54 (2019).
Daniels, T. R. et al. The transferrin receptor and the targeted delivery of therapeutic agents against cancer. Biochim. Biophys. Acta 1820, 291–317 (2012).
Hogemann-Savellano, D. et al. The transferrin receptor: a potential molecular imaging marker for human cancer. Neoplasia 5, 495–506 (2003).
Hopkins, C. R., Miller, K. & Beardmore, J. M. Receptor-mediated endocytosis of transferrin and epidermal growth factor receptors: a comparison of constitutive and ligand-induced uptake. J. Cell Sci. Suppl. 3, 173–186 (1985).
Hsu, V. W., Bai, M. & Li, J. Getting active: protein sorting in endocytic recycling. Nat. Rev. Mol. Cell Biol. 13, 323–328 (2012).
Shaul, Y. D. et al. MERAV: a tool for comparing gene expression across human tissues and cell types. Nucleic Acids Res. 44, D560–D566 (2016).
Schmiedel, B. J. et al. Impact of genetic polymorphisms on human immune cell gene expression. Cell 175, 1701–1715 e1716 (2018).
Klesmith, J. R. et al. Retargeting CD19 chimeric antigen receptor T cells via engineered CD19-fusion proteins. Mol. Pharm. 16, 3544–3558 (2019).
Naqvi, S. A. et al. Insertion of a lysosomal enzyme cleavage site into the sequence of a radiolabeled neuropeptide influences cell trafficking in vitro and in vivo. Cancer Biother. Radiopharm. 25, 89–95 (2010).
Poreba, M. Protease-activated prodrugs: strategies, challenges, and future directions. FEBS J. 287, 1936–1969 (2020).
Anami, Y. et al. Glutamic acid-valine-citrulline linkers ensure stability and efficacy of antibody-drug conjugates in mice. Nat. Commun. 9, 2512 (2018).
Goenaga, A. L. et al. Identification and characterization of tumor antigens by using antibody phage display and intrabody strategies. Mol. Immunol. 44, 3777–3788 (2007).
Tillotson, B. J., Goulatis, L. I., Parenti, I., Duxbury, E. & Shusta, E. V. Engineering an anti-transferrin receptor ScFv for pH-sensitive binding leads to increased intracellular accumulation. PLoS ONE 10, e0145820 (2015).
Santomasso, B., Bachier, C., Westin, J., Rezvani, K. & Shpall, E. J. The other side of CAR T-Cell therapy: cytokine release syndrome, neurologic toxicity, and financial burden. Am. Soc. Clin. Oncol. Educ. Book 39, 433–444 (2019).
Brandt, L. J. B., Barnkob, M. B., Michaels, Y. S., Heiselberg, J. & Barington, T. Emerging approaches for regulation and control of CAR T cells: a mini review. Front. Immunol. 11, 326 (2020).
Herbst, R. S. et al. Atezolizumab for first-line treatment of PD-L1-selected patients with NSCLC. N. Engl. J. Med. 383, 1328–1339 (2020).
Friedman, M. et al. Directed evolution to low nanomolar affinity of a tumor-targeting epidermal growth factor receptor-binding affibody molecule. J. Mol. Biol. 376, 1388–1402 (2008).
Pierpont, T. M., Limper, C. B. & Richards, K. L. Past, present, and future of rituximab-the world’s first oncology monoclonal antibody therapy. Front. Oncol. 8, 163 (2018).
Huotari, J. & Helenius, A. Endosome maturation. EMBO J. 30, 3481–3500 (2011).
Fu, H., Jiang, Y., Wong, W. P. & Springer, T. A. Single-molecule imaging of von Willebrand factor reveals tension-dependent self-association. Blood 138, 2425–2434 (2021).
Kobayashi, S. et al. EGFR mutation and resistance of non-small-cell lung cancer to gefitinib. N. Engl. J. Med. 352, 786–792 (2005).
Sequist, L. V. et al. Genotypic and histological evolution of lung cancers acquiring resistance to EGFR inhibitors. Sci. Transl. Med. 3, 75ra26 (2011).
Yu, H. A. et al. Analysis of tumor specimens at the time of acquired resistance to EGFR-TKI therapy in 155 patients with EGFR-mutant lung cancers. Clin. Cancer Res. 19, 2240–2247 (2013).
Cross, D. A. et al. AZD9291, an irreversible EGFR TKI, overcomes T790M-mediated resistance to EGFR inhibitors in lung cancer. Cancer Discov. 4, 1046–1061 (2014).
Leonetti, A. et al. Resistance mechanisms to osimertinib in EGFR-mutated non-small cell lung cancer. Br. J. Cancer 121, 725–737 (2019).
Thress, K. S. et al. Acquired EGFR C797S mutation mediates resistance to AZD9291 in non-small cell lung cancer harboring EGFR T790M. Nat. Med. 21, 560–562 (2015).
Ercan, D. et al. Amplification of EGFR T790M causes resistance to an irreversible EGFR inhibitor. Oncogene 29, 2346–2356 (2010).
Haikala, H. M. et al. EGFR inhibition enhances the cellular uptake and antitumor-activity of the HER3 antibody-drug conjugate HER3-DXd. Cancer Res. 82, 130–141 (2022).
Cho, J. et al. Cetuximab response of lung cancer-derived EGF receptor mutants is associated with asymmetric dimerization. Cancer Res. 73, 6770–6779 (2013).
Kurppa, K. J. et al. Treatment-induced tumor dormancy through YAP-mediated transcriptional reprogramming of the apoptotic pathway. Cancer Cell 37, 104–122 e112 (2020).
Richard, C. & Verdier, F. Transferrin receptors in erythropoiesis. Int. J. Mol. Sci. 21, 9713 (2020).
Kim, B. J. et al. Transferrin fusion technology: a novel approach to prolonging biological half-life of insulinotropic peptides. J. Pharmacol. Exp. Ther. 334, 682–692 (2010).
Su, L. Y. et al. Anti-tumor immunotherapy using engineered bacterial outer membrane vesicles fused to lysosome-targeting chimeras mediated by transferrin receptor. Cell. Chem. Biol. https://doi.org/10.1016/j.chembiol.2024.01.002 (2024).
Giovannini, M. et al. Clinical significance of skin toxicity due to EGFR-targeted therapies. J. Oncol. 2009, 849051 (2009).
Pulgar, V. M. Transcytosis to cross the blood brain barrier, new advancements and challenges. Front. Neurosci. 12, 1019 (2018).
Sonoda, H. et al. A blood-brain-barrier-penetrating anti-human transferrin receptor antibody fusion protein for neuronopathic mucopolysaccharidosis II. Mol. Ther. 26, 1366–1374 (2018).
Okuyama, T. et al. A phase 2/3 trial of pabinafusp alfa, IDS fused with anti-human transferrin receptor antibody, targeting neurodegeneration in MPS-II. Mol. Ther. 29, 671–679 (2021).
Niewoehner, J. et al. Increased brain penetration and potency of a therapeutic antibody using a monovalent molecular shuttle. Neuron 81, 49–60 (2014).
Hultqvist, G., Syvanen, S., Fang, X. T., Lannfelt, L. & Sehlin, D. Bivalent brain shuttle increases antibody uptake by monovalent binding to the transferrin receptor. Theranostics 7, 308–318 (2017).
Liu, R., Oldham, R. J., Teal, E., Beers, S. A. & Cragg, M. S. Fc-engineering for modulated effector functions-improving antibodies for cancer treatment. Antibodies 9, 64 (2020).
Wang, X., Mathieu, M. & Brezski, R. J. IgG Fc engineering to modulate antibody effector functions. Protein Cell 9, 63–73 (2018).
Yamin, R. et al. Fc-engineered antibody therapeutics with improved anti-SARS-CoV-2 efficacy. Nature 599, 465–470 (2021).
Saunders, K. O. Conceptual approaches to modulating antibody effector functions and circulation half-life. Front. Immunol. 10, 1296 (2019).
Roth, T. L. et al. Reprogramming human T cell function and specificity with non-viral genome targeting. Nature 559, 405–409 (2018).