Extension of TAGLN2 half-life via ubiquitination site mutation

Abstract

The upward tendency focus on immunotherapeutics which has been regarded as an efficient way for tumor clearance. However, despite the pervasiveness of immunotherapeutics regimens such as genetically engineered T cells, immune checkpoint blockade and tumor vaccine, competence to elicit the complete remission still remains poor. Although T cells could adequately infiltrate into tumor region, recognition of target is inhibited by TME (tumor microenvironment), which can hinder immune synapse formation via reducing the avidity between tumor cells and TILs (Tumor Infiltrating Lymphocyte). Therefore, to encourage the target recognition, and to maximize the immune response, it is desirable to increase the avidity of TILs. Thus, we examined the actin binding protein TAGLN2 tagged peptide transfer domain to enforce the immune response against tumor. This small 22 kDa, TAGLN2, has been identified as actin cross-linking/gelling protein in our previous results, and it functioned as an immune stabilizer by potentiating the avidity. Here, we suggest mutated TAGLN2 as supporter of conventional immunotherapeutics for overcoming immunosuppressive meliu surrounding tumor region.