File Name: tak1 is a ubiquitin dependent kinase of mkk and ikk .zip
- Ubiquitin-mediated activation of TAK1 and IKK
- TAK1 Is A Ubiquitin-dependent Kinase Of MKK And IKK
- The IKK Complex, a Central Regulator of NF-κB Activation
Ubiquitin-mediated activation of TAK1 and IKK
William W. Tewalt, Timothy O. Leonard, Christopher C. J Exp Med 11 June ; 6 : — The deubiquitinating enzyme CYLD has recently been implicated in the regulation of signal transduction, but its physiological function and mechanism of action are still elusive. In this study, we show that CYLD plays a pivotal role in regulating T cell activation and homeostasis.
TAK1 Is A Ubiquitin-dependent Kinase Of MKK And IKK
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The IKK Complex, a Central Regulator of NF-κB Activation
Thus, TRAFs possess important and complex signaling functions in the immune system and play an important role in regulating immune and inflammatory responses. The TRAF domain mediates oligomerization of TRAF proteins as well as their association with upstream receptors or adaptors and downstream effector proteins 1. The RING domain is best known for its function to mediate protein ubiquitination in a large family of E3 ubiquitinase ligases 3. TRAF6 is a well-characterized E3 ligase that specifically conjugates lysine K linked polyubiquitin chains 4.
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Additional components may exist, transiently or permanently, but their characterization is still unsure. I will review here the genetic, biochemical, and structural data accumulated during the last 10 yr regarding the function of the three IKK subunits. This modification allows their polyubiquitination and destruction by the proteasome. The kinase subunits. The function of the leucine zipper domain is to allow homo- or heterodimerization of the kinases. The role of the helix loop helix domain is less clear, but it seems to be involved in the modulation of the kinase activity. The exact mechanism by which the kinase subunits become activated remains obscure.
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