IndraLab

Statements

CASP8 inhibits CYLD. 31 / 35
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"Since caspase 8 is not recruited to the membrane-anchored TNFR-1 complex where CYLD is supposed to exert its effect [ xref , xref ], caspase 8 should not be able to cleave and inhibit CYLD at this complex."
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"Active caspase-8 has been reported to inhibit necroptosis by cleaving RIPK1, RIPK3, and CYLD XREF_BIBR - XREF_BIBR."
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"It has recently been shown that during embryogenesis and T-cell proliferation active pro apoptotic caspase-8 blocks necroptosis by processing CYLD XREF_BIBR, XREF_BIBR, which is consistent with our findings of cross regulation of death pathways by caspase-1 activity."
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"Furthermore, within Complex IIa, activated caspase-8 cleaves and inactivates RIP1, RIP3, and CYLD."
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"Neither RIPK1 nor RIPK3 was required for the processing of CYLD to CYLDp25 in MEFs ( xref ), indicating that CASPASE 8 inactivation of CYLD occurs upstream of these necrosome components."
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"Caspase-8 inhibits necroptosis by cutting RIPK1, RIPK3, and cylindromatosis (CYLD)."
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"Caspase-8 can cleave and inactivate CYLD, a tumor suppressor protein that deubiquitinates the M1 and K63 ubiquitin chains in RIG-I and TAK1 [ xref – xref ]."
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"It is suggested that increased cFLIP may promote caspase 8-mediated degradation of CYLD and other necrosomal components, potentially abrogating MTB-induced necroptotic signaling [96]."
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"In contrast, loss of CASPASE 8 prevented CYLD degradation resulting in necrotic death."
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"The unexpected role for RIP3 in promoting caspase-8 modification and activity also implies that RIP3 facilitates a negative feedback loop, because active caspase-8 can process and possibly inactivate [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Co-transfection of HEK 293 cells revealed that over-expression of wild-type CASPASE 8, but not the catalytically inactive mutant CASPASE 8-C360S, causes degradation of CYLD protein (XREF_FIG)."
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"Neither RIPK1 nor RIPK3 were required for CYLD cleavage, and CYLD inactivation by casp8 is proposed to occur upstream of RIPK activity."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, a deubiquitinase that removes K63-linked ubiquitin from RIG-I. Caspase-8 knockout and Z-Vad blocked PEDV-induced RIG-I K63 ubiquitination."
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"Caspase-8 inhibits the initiation of necroptosis by cleaving and inactivating RIP1, RIP3 [XREF_BIBR] and deubiquitinase CYLD, which was shown to be required for necroptosis induction [XREF_BIBR]."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, leading to increased RIG-I and TAK1 ubiquitination and antiviral responses (Fig. 9E)."
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"Neither RIPK1 nor RIPK3 were required for CYLD cleavage, and CYLD inactivation by casp8 is proposed to occur upstream of RIPK activity."
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"Neither RIPK1 nor RIPK3 was required for the processing of CYLD to CYLDp25 in MEFs (XREF_SUPPLEMENTARY), indicating that CASPASE 8 inactivation of CYLD occurs upstream of these necrosome components."
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"We identified cFLIP upregulation that may promote caspase 8 mediated degradation of CYLD, and other necrosome components, as a possible mechanism abrogating Mtb 's capacity to coopt necroptotic signaling."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, leading to increased RIG-I and TAK1 ubiquitination and antiviral responses (Fig.  xref E)."
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"Under conditions of cellular stress, and when the magnitude of the trigger is sufficient to suppress the downstream NF-κB mediated survival queues, CASPASE-8 inhibits RIPK1 and CYLD and activates the effector caspases CASPASE 3/7, leading to apoptotic death."
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"The crucial function of CYLD in necroptosis was further supported by the observation that caspase-8 inactivates CYLD by proteolytic cleavage, which restricts necroptosis upon apoptosis induction [161][MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Caspase-8 can cleave and inactivate CYLD, a tumor suppressor protein that deubiquitinates the M1 and K63 ubiquitin chains in RIG-I and TAK1 [14–17]."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, a deubiquitinase that removes K63-linked ubiquitin from RIG-I."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, a tumor suppressor that functions as a deubiquitinase."
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"Caspase 8 then cleaves and inactivates RIPK1, RIPK3 and CYLD and stimulates apoptosis."
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"When caspase 8 is not inhibited, or if RIP3 is expressed at low enough levels, caspase 8 antagonizes necrosis by cleaving and inactivating RIP1, RIP3, and CYLD [35–39] , effectively terminating the ne[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Under conditions of cellular stress, and when the magnitude of the trigger is sufficient to suppress the downstream NF-κB mediated survival queues, CASPASE-8 inhibits RIPK1 and CYLD and activates the effector caspases CASPASE 3/7, leading to apoptotic death."
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"The apoptotic caspase-8 typically blocks necroptosis by cleaving RIPK3, CYLD, and RIPK1 [62,63,64]."
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"In turn, caspase-8 can cleave and inactivate CYLD ( xref ), thus forming a negative feedback loop that enables a balance between pro-survival and pro-apoptotic processes."
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"Mechanistically, caspase-8 cleaves and inactivates CYLD, a tumor suppressor that functions as a deubiquitinase."
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"Caspase-8 suppresses necroptosis by cleaving CYLD [101] ."
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