IndraLab

Statements

DDX58 binds CYLD. 22 / 24
1 1 | 5 15
sparser
"In a yeast two-hybrid screen, SDC4 was identified as a RIG-I interacting protein that promotes the binding of RIG-I with CYLD in order to decrease K63-linked ubiquitination ( xref )."
32117959
sparser
"SDC4 likely promotes redistribution of RIG-I and CYLD in a perinuclear pattern post viral infection, and thus enhances the RIG-I–CYLD interaction and potentiates the K63-linked deubiquitination of RIG-I. Collectively, our findings uncover a mechanism by which SDC4 antagonizes the activation of RIG-I in a CYLD-mediated deubiquitination-dependent process, thereby balancing antiviral signalling to avoid deleterious effects on host cells."
27279133
sparser
"Here the authors show that Syndecan-4 via its cytosolic domain negatively regulates antiviral immunity by enhancing RIG-I interaction with a deubiquitinating enzyme CYLD, thus inhibiting the activating K63-linked RIG-I ubiquitination."
27279133
sparser
"Interestingly, SDC4ΔC was also unable to bind CYLD ( xref ), which indicates that the CP region of SDC4 is necessary for its interaction with either RIG-I or CYLD."
27279133
reach
"CYLD binds to RIG-I and inhibits the ubiquitination and signaling function of RIG-I XREF_BIBR, XREF_BIBR."
27012466
sparser
"As shown in xref , similar to the sub-cellular pattern of RIG-I, SDC4 and CYLD were also accumulated in a perinuclear pattern on SeV infection, raising a possibility that SDC4 has a potential role in affecting the RIG-I–CYLD interaction and their perinuclear localization as well."
27279133
reach
"Newly synthesized SDC4 then recruits CYLD and RIG-I to form a large complex in the membrane compartment in a perinuclear pattern, which assists the interaction between CYLD and RIG-I, as well as the deubiquitination of the K63 linked ubiquitin of RIG-I."
27279133
sparser
"We provide extensive biochemical evidence to demonstrate that SDC4, via its carboxyl-terminal intracellular domain, interacts with RIG-I and CYLD, thereby facilitating the interaction between RIG-I and CYLD."
27279133
sparser
"USP4 and ovarian tumor-domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) stabilize RIG-I proteins by eliminating the K48-linked ubiquitin chains conjugated to RIG-I. xref , xref Conversely, CYLD , a tumor suppressor gene expressed in cylindromatosis, negatively regulates RIG-I activation by deubiquitinating the K63-linked ubiquitin chains on RIG-I. xref Moreover, syndecan-4 (SDC4), which is a TM protein, complexes with both RIG-I and CYLD to promote the CYLD-mediated deubiquitination of RIG-I, leading to subsequent signaling inhibition. xref Furthermore, USP3, xref USP21, xref USP14, xref and USP27X xref also deubiquitinate the K63-linked ubiquitin of RIG-I to inhibit RIG-I function."
33462384
sparser
"CYLD binds to RIG-I and inhibits the ubiquitination and signaling function of RIG-I xref , xref ."
27012466
sparser
"227 Moreover, syndecan-4 (SDC4), which is a TM protein, complexes with both RIG-I and CYLD to promote the CYLD-mediated deubiquitination of RIG-I, leading to subsequent signaling inhibition."
33462384
hprd
No evidence text available
18636086
sparser
"CYLD interacts with RIG-I and removes Lys63-linked polyubiquitin chains from it, which might be a mechanism involved in the downregulation of the IFN pathway42."
26061460
sparser
"Second, the effect mediated by SDC4 is specific on the RIG-I–CYLD interaction, because the RIG-I-TRIM25 association was not affected by SDC4 ( xref )."
27279133
sparser
"In a yeast two-hybrid screen, identifying a glycoprotein existing on the cell membrane, SDC4, interacts with RIG-I and CYLD through its carboxyl-terminal intracellular domain, promoting the deubiquitylation of RIG-I by CYLD and facilitating viral replication."
34966378
sparser
"Newly synthesized SDC4 then recruits CYLD and RIG-I to form a large complex in the membrane compartment in a perinuclear pattern, which assists the interaction between CYLD and RIG-I, as well as the deubiquitination of the K63-linked ubiquitin of RIG-I. Importantly, we found that a carboxyl-terminal fragment of SDC4 containing only 28 amino-acid residues was essential for the inhibitory function of SDC4."
27279133
biogrid
No evidence text available
18636086
sparser
"A recent study reported that SDC4 enhances the interaction between CYLD and RIG-I, thus promoting the removal of K63-linked polyubiquitin chains on RIG-I [ xref ]."
30388174
sparser
"CYLD binds to RIG1 and thereby inhibits ubiquitylation and signalling functions of RIG1."
28959952
reach
"We provide extensive biochemical evidence to demonstrate that SDC4, via its carboxyl-terminal intracellular domain, interacts with RIG-I and CYLD, thereby facilitating the interaction between RIG-I and CYLD."
27279133
reach
"First, our co-IP experiments showed that SDC4 overexpression indeed enhanced the interaction between CYLD and RIG-I, whereas SDC4 knockdown reduced the association of CYLD with RIG-I (XREF_FIG)."
27279133
reach
"CYLD physically interacts with both RIG-I and MAVS and preferentially inhibits the ubiquitination of RIG-I [XREF_BIBR] along with TBK1 and IKKepsilon, upregulating several IFN stimulating genes."
33138315