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| Content Provider | frontiers |
|---|---|
| Author | Wang, Qi-Long Liang, Jia-Qi Gong, Bei-Ni Xie, Ji-Ji Yi, Yu-Ting Lan, Xin Li, Yingqiu |
| Abstract | The SUMO modification system plays an important role in T cell activation, yet how sumoylation regulates TCR-proximal signalling remains largely unknown. We show here that Phospholipase C-γ1 (PLC-γ1) is conjugated by SUMO1 at K54 and K987 upon TCR stimulation and that K54 sumoylation is pivotal for PLC-γ1-mediated T cell activation. We further demonstrate that TCR-induced K54 sumoylation of PLC-γ1 significantly promotes the formation of PLC-γ1 microclusters and the association of PLC-γ1 with the adaptor proteins SLP76 and Gads,but only slightly affects the phosphorylation of PLC-γ1 on Y783, which determines the enzyme catalytic activity. Moreover, upon TCR stimulation, the SUMO E3 ligases PIASxβ and PIAS3 both interact with PLC-γ1 and cooperate to sumoylate PLC-γ1, facilitating the assembly of PLC-γ1 microclusters. Together, our findings reveal a critical role of PLC-γ1 K54 sumoylation in PLC-γ1 microcluster assembly that controls PLC-γ1-mediated T cell activation, suggesting that sumoylation may have an important role in the microcluster assembly of TCR-proximal signalling proteins. |
| ISSN | 16643224 |
| DOI | 10.3389/fimmu.2019.00314 |
| Volume Number | 10 |
| Journal | Frontiers in Immunology |
| Language | English |
| Publisher Date | 2019-02-28 |
| Access Restriction | Open |
| Subject Keyword | Sumoylation Microcluster Tcr-proximal signaling PIAS SUMO E3 PLC-γ1 |
| Content Type | Text |
| Resource Type | Article |
| Subject | Immunology and Allergy Immunology |
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