Tim-3 is a transmembrane protein that is highly expressed on subsets of chronically stimulated CD4+ helper and CD8+ cytotoxic T cells, with more transient expression during acute activation and infection. Tim-3 is also constitutively expressed by multiple types of myeloid cells. Like other TIM family members, Tim-3 can bind to phosphatidylserine displayed by apoptotic cells, and this interaction has been shown to mediate uptake of such cells by dendritic cells and cross-presentation of antigens to CD8+ T cells. In contrast, how the recognition of PS by Tim-3 might regulate the function of Tim-3+ T cells is not known. In their recent paper, Lemmon and colleagues demonstrate for the first time that recognition of PS by Tim-3 leads to enhanced T cell activation.
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November 2021
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In this issue, Chattopadhyay and colleagues (pp. 4027–4043) determine that obesity-induced FetA acts as a master upstream regulator of AT inflammation by regulating MCP-1 and iNOS expression through JNK-cJun-IFNγ-JAK2-STAT1 signalling pathway. The cover image shows Stromal vascular fraction (SVF) isolated from SD, HFD and HFD + FetAKD mice subjected to iNOS, CD11c and Arginase 1 immunoblotting. Image courtesy of Sutapa Mukherjee.
Commentary|
November 23 2021
Regulation of Tim-3 function by binding to phosphatidylserine
Lawrence P. Kane
Department of Immunology, University of Pittsburgh, Pittsburgh, PA 15261, U.S.A
Correspondence: Lawrence P. Kane (lkane@pitt.edu)
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Biochem J (2021) 478 (22): 3999–4004.
Article history
Received:
September 30 2021
Revision Received:
October 27 2021
Accepted:
October 29 2021
Connected Content
This is a commentary on:
Phosphatidylserine binding directly regulates TIM-3 function
Citation
Lawrence P. Kane; Regulation of Tim-3 function by binding to phosphatidylserine. Biochem J 26 November 2021; 478 (22): 3999–4004. doi: https://doi.org/10.1042/BCJ20210652
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