IndraLab

Statements

RIPK1 activates CYLD. 4 / 4
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"25 , 28 , 29 Additionally, RIPK1’s scaffold function can sub-lethally activate caspase-8, which in turn cleaves and inactivates RIPK3, cylindromatosis lysine 63 deubiquitinase (CYLD), and RIPK1 itself[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
38788712
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"The intimate involvement of CYLD in necrotic death was elucidated in a landmark paper by Moquin and colleagues that detailed CYLD mediated regulation of TNFalpha induced necrosis by deubiquitination of RIPK1 in MEF and L929 cells, while, conversely, CYLD downregulation by Toll Like Receptors protects mouse macrophages from necrosis [XREF_BIBR, XREF_BIBR]."
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"79 RIPK1 autophosphorylation following DD-mediated dimerization of the kinase 80 licenses RIPK1 to enter a secondary, cytoplasmic death-inducing complex II. 81 Transition of RIPK1 from complex I to co[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, CYLD- and A20-driven deubiquitination of RIP1 have been variously reported as pro- and antinecroptotic in different cell types: some studies have shown that CYLD drives RIP1 deubiquitination (11,17,19,20), while others have implicated A20 (13,21,22) or reported equal contributions from both enzymes (23,24,25)."
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