Endoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 is a novel substrate of MK2 (MAPKAP kinase-2) involved in MK2-mediated TNFα production

2013 ◽  
Vol 456 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Manoj B. Menon ◽  
Christopher Tiedje ◽  
Juri Lafera ◽  
Natalia Ronkina ◽  
Timo Konen ◽  
...  
Keyword(s):  
Immune Response ◽  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Tumour Necrosis ◽  
Innate Immune ◽  
Tumour Necrosis Factor Α ◽  
Ubiquitin Conjugating Enzyme ◽  
Factor Α ◽  
Necrosis Factor ◽  
Conjugating Enzyme

The protein kinase MK2 phosphorylates the endoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 under various stress conditions and during the innate immune response in macrophages. Although its apparent enzyme activity stays unaltered, Ube2j1 contributes to MK2-dependent biosynthesis of tumour necrosis factor α.

scholarly journals Deletion of tumour necrosis factor α receptor 1 elicits an increased TH17 immune response in the chronically inflamed liver

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Laura Berkhout ◽  
Roja Barikbin ◽  
Birgit Schiller ◽  
Gevitha Ravichandran ◽  
Till Krech ◽  
...  
Keyword(s):  
Immune Response ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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