Optimization of a capsid integrity RT-qPCR method to quantify thermally inactivated hepatitis E virus in suspensions and in deli meat samples

Audrey Fraisse

doi:10.1016/j.fm.2026.105193

MARCH2 mediates K27-Linked polyubiquitination of IL-2 receptor α to negatively regulate T cell proliferation

2026-04-01

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PRE

AI

M

Ma, Zhen-Wu

Z

Zhang, Qi

S

Shi, Jun-Ge

L

Li, Shu

DOI：10.1093/jimmun/vkag045

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Interleukin 2 (IL-2) is a cytokine secreted by activated T cells that plays a central role in T cell proliferation and differentiation. In this study, we identified MARCH2, an E3 ubiquitin ligase of the MARCH family, as a negative regulator of IL-2 receptor alpha (IL-2R alpha). MARCH2 interacts with IL-2R alpha and catalyzes its K27-linked polyubiquitination and subsequent proteasomal degradation. Site-directed mutagenesis indicates that K267 of IL-2R alpha is targeted by MARCH2 and mutation of this residue impairs MARCH2-mediated polyubiquitination and degradation of IL-2R alpha. MARCH2-deficiency promotes IL-2-triggered STAT5 phosphorylation, effector gene expression, and proliferation of activated T cells. Our findings suggest that MARCH2 negatively regulates IL-2 signaling by targeting IL-2R alpha for K27-linked polyubiquitination and proteasomal degradation, uncovering a post-translational mechanism that regulates T cell homeostasis.

Keywords:

IL-2R alpha

MARCH2

polyubiquitination

T cell proliferation

MARCH2 mediates K27-Linked polyubiquitination of IL-2 receptor α to negatively regulate T cell proliferation

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