Detection of protein posttranslational modifications by mass spectrometry

Author(s):  
Arnold Steckel ◽  
Katalin Uray ◽  
Gitta Schlosser
2012 ◽  
Vol 421 (2) ◽  
pp. 517-525 ◽  
Author(s):  
Quanzhou Luo ◽  
Jette Wypych ◽  
Xinzhao Grace Jiang ◽  
Xin Zhang ◽  
Shun Luo ◽  
...  

2012 ◽  
Vol 421 (2) ◽  
pp. 506-516 ◽  
Author(s):  
Xinzhao Grace Jiang ◽  
Izydor Apostol ◽  
Quanzhou Luo ◽  
Jeffrey Lewis ◽  
Ronald Keener ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Peng Gao ◽  
Xianwei Ma ◽  
Ming Yuan ◽  
Yulan Yi ◽  
Guoke Liu ◽  
...  

AbstractUbiquitination is one of the most prevalent protein posttranslational modifications. Here, we show that E3 ligase Nedd4l positively regulates antiviral immunity by catalyzing K29-linked cysteine ubiquitination of TRAF3. Deficiency of Nedd4l significantly impairs type I interferon and proinflammatory cytokine production induced by virus infection both in vitro and in vivo. Nedd4l deficiency inhibits virus-induced ubiquitination of TRAF3, the binding between TRAF3 and TBK1, and subsequent phosphorylation of TBK1 and IRF3. Nedd4l directly interacts with TRAF3 and catalyzes K29-linked ubiquitination of Cys56 and Cys124, two cysteines that constitute zinc fingers, resulting in enhanced association between TRAF3 and E3 ligases, cIAP1/2 and HECTD3, and also increased K48/K63-linked ubiquitination of TRAF3. Mutation of Cys56 and Cys124 diminishes Nedd4l-catalyzed K29-linked ubiquitination, but enhances association between TRAF3 and the E3 ligases, supporting Nedd4l promotes type I interferon production in response to virus by catalyzing ubiquitination of the cysteines in TRAF3.


2014 ◽  
Vol 8 (7-8) ◽  
pp. 543-553 ◽  
Author(s):  
Genaro A. Ramirez-Correa ◽  
Maria Isabel Martinez-Ferrando ◽  
Pingbo Zhang ◽  
Anne M. Murphy

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