Protein 4.1R negatively regulates CD8+ T‐cell activation by modulating phosphorylation of linker for activation of T cells

• DOI: 10.1111/imm.13085
• Publication Date: 2019-05-28T14:59:53Z
• Authors: Dandan Fan; Jianhui Li; Yi Li; Yaxin Guo; Xiaolin Zhang; Wen Wang; Xiaojie Liu; Jingjing Liu; Liping Dai; Liguo Zhang; Qiaozhen Kang; Zhenyu Ji
• Keywords: Immunoprecipitation; Jurkat cells

Protein 4.1R, an 80 000 MW membrane skeleton protein, is a vital component of the red blood cell cytoskeleton that stabilizes spectrin-actin network and regulates properties deformability mechanical stability. It has been shown 4.1R expressed in T cells, including CD8+ but its role cells remains unclear. Here, we have explored using 4.1R-/- mice. Our results showed activation, proliferation secretion levels interleukin-2 interferon-γ were significantly increased cells. Furthermore, phosphorylation linker for activation (LAT) downstream signaling molecule extracellular signal-regulated kinase enhanced absence 4.1R. In vitro co-immunoprecipitation experiments direct interaction between LAT. Moreover, mice exhibited T-cell-dependent immune response. These data enabled identification negative regulation function by association LAT, possibly through inhibiting LAT then modulating intracellular signal transduction.