IndraLab

Statements


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sparser
"While OTULIN binds HOIP directly through its PUB-interacting motif (PIM) ( xref , xref ), CYLD is recruited via a PIM in the bridging factor SPATA2 ( xref , xref , xref , xref )."

sparser
"The specificity of the HOIP PUB-OTULIN interaction stems from a binding preference of the HOIP PIM pocket for internal PIMs in contrast to the C-terminal PIM of p97/VCP [ xref , xref ]."

sparser
"OTULIN interacts with the N-terminal PUB domain of HOIP via an evolutionarily conserved PUB-interacting motif to remove the Met-1 Ub on IKKγ [ xref – xref ], thus leading to the inactivation of IKK."

sparser
"OTULIN interacts with the N-terminal PUB domain of HOIP via an evolutionarily conserved PUB-interacting motif ( xref )."

sparser
"To test that OTULIN indeed directly binds to the Ψ–Y pocket of HOIP, we introduced various point mutations and detected a decrease in OTULIN binding to the HOIP PUB domain with both single mutants Y82[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Now, we show that OTULIN binds via a conserved PUB-interacting motif (PIM) to the PUB domain of the LUBAC component HOIP."

sparser
"Mass spectrometry and biochemical analysis showed that OTULIN binds to the HOIP PUB (peptide: N-glycanase/UBA- or UBX-containing proteins) domain [ xref , xref ]."

sparser
"OTULIN contains a PIM sequence and is bound directly by HOIP-PUB [ xref , xref ]."

sparser
"OTULIN binds to the PUB domain of HOIP and loss of HOIP-OTULIN interaction reduces OTULIN’s capacity to restrict LUBAC-induced immune responses [ xref ]."

sparser
"Crystal structures and nuclear magnetic resonance experiments reveal the molecular basis for the high-affinity interaction and explain why OTULIN binds the HOIP PUB domain specifically."