IndraLab

Statements


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sparser
"Given that RIPK2 was identified as a YOD1-interacting protein by mass spectrometry (Fig.  xref ) and that YOD1 critically regulated RIPK2 stability (Fig.  xref ; Appendix Fig.  xref ), we assessed the direct interaction between YOD1 and RIPK2 by co-immunoprecipitation and western blot."

sparser
"The co-IP result showed that the YOD1 mutant lacking the UBXL domain failed to interact with RIPK2, showing that YOD1 binds RIPK2 through the UBXL domain (Fig.  xref )."

sparser
"In this study, we demonstrate that YOD1 interacts with RIPK2 through the UBXL domain."

sparser
"Recent research indicates that YOD1 binds to RIPK2 via its UBXL domain and increases the abundance of RIPK2 by reducing K48 polyubiquitination and proteasomal degradation of RIPK2, thereby enhancing NOD2 signaling and exerting a protective role in promoting physiological inflammatory responses in macrophages [ xref ]."

reach
"YOD1 binds and K48 deubiquitinates RIPK2."

reach
"Given that RIPK2 was identified as a YOD1-interacting protein by mass spectrometry (Fig. 5B) and that YOD1 critically regulated RIPK2 stability (Fig. 5D–H; Appendix Fig. S12), we assessed the direct interaction between YOD1 and RIPK2 by co-immunoprecipitation and western blot."