negative regulation of ripoptosome assembly involved in necroptotic process

Definition

Target type: biologicalprocess

Any process that stops, prevents or reduces the frequency, rate or extent of ripoptosome assembly involved in a necroptotic process. [GOC:dph, GOC:mtg_apoptosis, GOC:TermGenie, PMID:21052097]

Necroptosis is a programmed form of cell death that is distinct from apoptosis. It is characterized by the formation of a large protein complex called the ripoptosome, which is responsible for activating the executioner caspase-8 and triggering the apoptotic cascade. However, in some cases, the ripoptosome can be negatively regulated to prevent necroptosis. This negative regulation is a complex process involving a number of different proteins and pathways.

One important mechanism for negative regulation of ripoptosome assembly is through the inhibition of RIPK1 kinase activity. RIPK1 is a key component of the ripoptosome and its kinase activity is essential for the formation of the complex. A number of proteins can inhibit RIPK1 kinase activity, including CYLD, A20, and cIAP1/2. These proteins can deubiquitinate RIPK1, which prevents its association with the ripoptosome.

Another mechanism for negative regulation of ripoptosome assembly is through the recruitment of the anti-apoptotic protein FLIP. FLIP is a caspase-8 inhibitor, and it can bind to RIPK1 and prevent the activation of caspase-8 by the ripoptosome.

Finally, the formation of the ripoptosome can also be negatively regulated by the ubiquitin-proteasome system. The ripoptosome is a large protein complex that is very unstable, and it can be rapidly degraded by the proteasome. This degradation is mediated by the ubiquitination of RIPK1, which targets it for proteasomal degradation.

In summary, the negative regulation of ripoptosome assembly is a complex process that involves multiple proteins and pathways. This negative regulation is essential for preventing necroptosis, and it is dysregulated in a number of diseases, including cancer and inflammation.'
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Proteins (1)

Compounds (8)