IndraLab

Statements


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reach
"CYLD, a de-ubiquitinating enzyme, physically interacts with p62, the CYLD and TRAF6 complex negatively regulates TRAF6 ubiquitination and regulates the sustained inhibitory actions of NF-kB and NFATc1 during RANKL induced osteoclastogenesis."

reach
"XREF_BIBR, XREF_BIBR Interestingly, there is also evidence that p62 interacts with CylD, which suggests a potential dual role of p62 in regulating not only the ubiquitination and subsequent activation of NF-kappaB signaling intermediaries but also its inactivation by deubiquitination through CylD."

sparser
"CYLD, a de-ubiquitinating enzyme, physically interacts with p62, the CYLD/TRAF6 complex negatively regulates TRAF6 ubiquitination and regulates the sustained inhibitory actions of NF-kB and NFATc1 during RANKL-induced osteoclastogenesis ( xref ). xref demonstrated that Sesn2 interacts with Keap1, p62, and ubiquitin ligase and that the antioxidant activity of Sesn2 is mediated by activation of Nrf2 and p62-dependent autophagic degradation of Keap1 when ROS is increased as a result of an increase in mTORC1 activity and ER stress due to environmental stresses."

No evidence text available

sparser
"As diagrammed in xref , whereas the p62-TRAF6 interaction was found immediately after IFN-γ/TLR stimulation, this interaction was largely replaced by the p62-CYLD interaction in a later stage, indicating that TRAF6 ubiquitination, triggered upon stimulation, was reversed at a later time, coinciding with the recruitment of CYLD."

reach
"Two recent studies have shown that the adaptor protein p62 (also named sequestosome 1) binds to CYLD and recruits it to TRAF6."

sparser
"To gain functional insight into the late interaction of p62 with CYLD, we examined ubiquitination of total p62- associated proteins following stimulation."

sparser
"Adaptor protein p62 binds to CYLD and recruits it to TRAF6 [ xref ]."

reach
"Moreover, p62, which interacted with TRAF6 in an early stage, interacted with CYLD, the deubiquitinating enzyme to the p62 complex, in a later stage."

sparser
"CYLD binds the scaffolding protein and autophagy receptor p62 [ xref ], which is also abundant in the PSD."

sparser
"Interestingly, we found that CYLD interacted physically with the signaling adaptor p62 and thereby was recruited to TRAF6."

reach
"CYLD interacts with p62 directly and CYLD can directly inactivate HDAC6, thereby controlling autophagy [XREF_BIBR]."

reach
"CYLD binds the scaffolding protein and autophagy receptor p62 [103], which is also abundant in the PSD."

sparser
"CYLD interacts with p62 directly and CYLD can directly inactivate HDAC6, thereby controlling autophagy [ xref ]."

sparser
"In xref , the interaction of p62 with CYLD was also seen in a reciprocal Co-IP after IFN-γ/ CpG stimulation."

reach
"These results reinforce the notion that p62, upon IFN-gamma and CpG induction, interacted with CYLD and inhibited TRAF6 autoubiquitination, leading to the negative regulation of NF-kappaB activity in macrophages."

reach
"The authors found that CYLD interacts directly with the adaptor protein p62 and is recruited to TRAF6 thereby leading to its deubiquitination and subsequent inhibition."

sparser
"Two recent studies have shown that the adaptor protein p62 (also named sequestosome 1) binds to CYLD and recruits it to TRAF6. xref , xref Whether p62 also recruits CYLD to other molecules is not known."

reach
"P62 interacts with CYLD and promotes the binding of CYLD to TRAF6, and this molecular interplay requires the C-terminal domain of p62 [XREF_BIBR]."

No evidence text available

sparser
"Here, we report that CYLD binds with the p62 wild-type (p62WT), non-UBA mutant (p62A381V) but not with the UBA mutant (p62P392L) in OCL progenitor cells."

sparser
"Thus, we examined the interaction of CYLD with p62 and autoubiquitination of TRAF6 following IFN-γ/CpG stimulation in RAW cells."

reach
"Adaptor protein p62 binds to CYLD and recruits it to TRAF6 [XREF_BIBR]."

sparser
"P62 interacts with CYLD and promotes the binding of CYLD to TRAF6, and this molecular interplay requires the C-terminal domain of p62 [ xref ]."

reach
"It has been shown that p62 and sequestosome1 binds to TRAF6 through its UBD and recruits CYLD to TRAF6 to regulate its ubiquitination XREF_BIBR, XREF_BIBR."

sparser
"The authors found that CYLD interacts directly with the adaptor protein p62 and is recruited to TRAF6 thereby leading to its deubiquitination and subsequent inhibition."

reach
"It has been shown that p62 and sequestosome1 binds to TRAF6 through its UBD and recruits CYLD to TRAF6 to regulate its ubiquitination XREF_BIBR, XREF_BIBR."