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Comment
. 2017 Dec;14(12):957-959.
doi: 10.1038/cmi.2017.91. Epub 2017 Sep 11.

Fine-tuning of thymocyte development by ubiquitination-mediated stability control of the ESCRT protein CHMP5

Masashi Watanabe  1 , Shigetsugu Hatakeyama  1
Affiliations
Comment

Fine-tuning of thymocyte development by ubiquitination-mediated stability control of the ESCRT protein CHMP5

Masashi Watanabe et al. Cell Mol Immunol. 2017 Dec.
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Models for post-translational control of CHMP5 during T-cell development. (a) When TCR is stimulated by low-affinity ligands, an unknown kinase activated by TCR signaling phosphorylates CHMP5 at Ser26 and Ser30, leading to recruitment of a deubiquitinating enzyme, USP8. USP8 stabilizes CHMP5 via its deubiquitination. Increased CHMP5 proteins directly bind to Bcl-2 and prevent reactive oxygen species (ROS)-mediated sulfenylation of Bcl-2 and subsequent degradation. These processes result in survival of thymocytes. (b) When TCR is stimulated by high-affinity ligands, CHMP5 is ubiquitinated and degraded via the proteasome pathway. CHMP5 proteins fail to prevent ROS-mediated sulfenylation and degradation of Bcl-2. These processes result in apoptosis of thymocytes. CHMP, charged MVB protein; TCR, T-cell receptor.
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