IndraLab

Statements


OTULIN binds RNF31 and PUB domain. 5 / 5
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reach
"Although HOIP is able to interact with the AAA ATPase p97 and valosin containing protein (VCP) [XREF_BIBR, XREF_BIBR], which has recently been implicated in the recruitment of LUBAC to misfolded Huntingtin species [XREF_BIBR], the HOIP PUB domain binds OTULIN with a 40-fold higher affinity compared to p97 and VCP and NMR based in vitro studies indicate a more stable interaction between HOIP and OTULIN compared to p97 and VCP [XREF_BIBR]."

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"Both DUBs interact with the LUBAC complex - OTULIN directly binds the PUB domain of the catalytic subunit HOIP, which then recruits it to the TNFR complex."

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"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."

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"Different from direct interaction between OTULIN and HOIP, CYLD binding to PUB domain of HOIP requires spermatogenesis-associated 2 (SPATA2) for bridge factor [23]."

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"OTULIN directly binds the PUB domain of HOIP to protect LUBAC from autoubiquitination, while CYLD associates with HOIP through Spermatogenesis-associated 2 (SPATA2) without affecting HOIP autoubiquiti[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"