Bridging the gap in protein targeting

Bridging the gap in protein targeting

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Access through your institution Buy or subscribe Targeted protein degradation has emerged as a highly promising therapeutic approach to modulate proteins that are difficult to target with conventional small molecules. This approach has recently been expanded to include alteration of extracellular protein levels and activity — including both secreted and membrane proteins. Now, Zhang et al. have exploited the upregulation of cell surface transferrin receptor 1 (TfR1) in cancer cells and its rapid endocytosis rate to develop transferrin receptor targeting chimeras (TransTACs). These are heterobispecific antibodies that induce internalization and lysosomal degradation of target membrane proteins. The team investigated the capacity of TransTACs to eliminate surface chimeric antigen receptor (CAR). Despite undergoing internalization, CAR is not subjected to degradation; instead, it is trafficked to the recycling endosomes. To address this the team incorporated an antibody binder to TfR1 and a cathepsin B cleavage linker to facilitate CAR entry into the lysosomal degradation pathway. CAR TransTACs can effectively inhibit the activation of Jurkat and human primary CAR T cells, as well as secretion of IFNγ. Furthermore, the target scope was expanded to include epidermal growth factor receptor (EGFR) for targeting drug-resistant lung cancer, as well as PD-L1 and CD20, demonstrating the capacity of TransTACs to efficiently internalize and degrade structurally and functionally distinct membrane proteins. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Access Nature and 54 other Nature Portfolio journals Get Nature+, our best-value online-access subscription $29.99 / 30 days cancel any time Learn more Subscribe to this journal Receive 12 print issues and online access $259.00 per year only $21.58 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Nature Communications https://www.nature.com/ncomms/ Irene Serrano Authors * Irene Serrano View author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Irene Serrano. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Serrano, I. Bridging the gap in protein targeting. _Nat Chem Biol_ 20, 1387 (2024). https://doi.org/10.1038/s41589-024-01766-3 Download citation * Published: 22 October 2024 * Issue Date: November 2024 * DOI: https://doi.org/10.1038/s41589-024-01766-3 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided by the Springer Nature SharedIt content-sharing initiative

Access through your institution Buy or subscribe Targeted protein degradation has emerged as a highly promising therapeutic approach to modulate proteins that are difficult to target with


conventional small molecules. This approach has recently been expanded to include alteration of extracellular protein levels and activity — including both secreted and membrane proteins.


Now, Zhang et al. have exploited the upregulation of cell surface transferrin receptor 1 (TfR1) in cancer cells and its rapid endocytosis rate to develop transferrin receptor targeting


chimeras (TransTACs). These are heterobispecific antibodies that induce internalization and lysosomal degradation of target membrane proteins. The team investigated the capacity of TransTACs


to eliminate surface chimeric antigen receptor (CAR). Despite undergoing internalization, CAR is not subjected to degradation; instead, it is trafficked to the recycling endosomes. To


address this the team incorporated an antibody binder to TfR1 and a cathepsin B cleavage linker to facilitate CAR entry into the lysosomal degradation pathway. CAR TransTACs can effectively


inhibit the activation of Jurkat and human primary CAR T cells, as well as secretion of IFNγ. Furthermore, the target scope was expanded to include epidermal growth factor receptor (EGFR)


for targeting drug-resistant lung cancer, as well as PD-L1 and CD20, demonstrating the capacity of TransTACs to efficiently internalize and degrade structurally and functionally distinct


membrane proteins. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Access Nature and 54 other Nature Portfolio journals


Get Nature+, our best-value online-access subscription $29.99 / 30 days cancel any time Learn more Subscribe to this journal Receive 12 print issues and online access $259.00 per year only


$21.58 per issue Learn more Buy this article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout


ADDITIONAL ACCESS OPTIONS: * Log in * Learn about institutional subscriptions * Read our FAQs * Contact customer support AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Nature Communications


https://www.nature.com/ncomms/ Irene Serrano Authors * Irene Serrano View author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence


to Irene Serrano. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Serrano, I. Bridging the gap in protein targeting. _Nat Chem Biol_ 20, 1387 (2024).


https://doi.org/10.1038/s41589-024-01766-3 Download citation * Published: 22 October 2024 * Issue Date: November 2024 * DOI: https://doi.org/10.1038/s41589-024-01766-3 SHARE THIS ARTICLE


Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided


by the Springer Nature SharedIt content-sharing initiative