IndraLab

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reach
"Next, a Co‐IP assay was conducted to examine the potential interaction between OTUB1 and RAB8A."

sparser
"Recent research has also found that OTUB1 maintains low levels of PD‐L1 ubiquitination, indicating its potential as a target in immune evasion related to PD‐L1/PD‐1 therapy and in the immunosuppression of cancer cells. [ xref , xref ] However, the interaction between OTUB1 and RAB8A in prostate cancer cells, and the role of circRNAs in this context, has not been reported."

reach
"We found that circ_0 005185 acts as a scaffold, facilitating the binding between the deubiquitinating enzyme OTUB1 and RAB8A and mediating their deubiquitination process, thereby stabilizing the protein levels of RAB8A and promoting primary cilium formation.Primary cilia are microtubule‐based organelles extending from the cell membrane that function as antennae to sense extracellular signals."

sparser
"The Co‐IP results demonstrated that OTUB1 can bind to RAB8A and that the overexpression of circ_0 005185 enhances this interaction."

reach
"Based on these observations, we hypothesized that circ_0 005185 mediates the deubiquitination of RAB8A by facilitating the binding of OTUB1 to RAB8A."

sparser
"Additionally, RNA pull‐down assays combined with mass spectrometry revealed that circ_0 005185 interacts with RAB8A and OTUB1."

sparser
"Based on these observations, we hypothesized that circ_0 005185 mediates the deubiquitination of RAB8A by facilitating the binding of OTUB1 to RAB8A. This mechanism subsequently regulates the formation of primary cilia and the activation of the Hh signaling pathway, ultimately influencing the progression and drug resistance of prostate cancer."

sparser
"Hsa_circ_0005185 interacts with OTUB1 and RAB8A, facilitating the binding of the deubiquitinating enzyme OTUB1 to RAB8A. This interaction promotes RAB8A deubiquitination, thereby stabilizing RAB8A. The stabilized RAB8A enhances primary cilia regeneration and increases the production of GLI3R, a known suppressor of Hedgehog signaling."

sparser
"Specifically, it is found that hsa_circ_0005185 interacts with OTUB1 and RAB8A, serving as a molecular scaffold."

sparser
"Hsa_circ_0005185 mediates the binding of the deubiquitinase OTUB1 to RAB8A, resulting in the deubiquitination of RAB8A. Consequently, the stable expression of RAB8A promotes the regeneration of primary cilia and enhances the production of GLI3R, an inhibitory factor in the Hedgehog signaling pathway, thereby suppressing AR activity and slowing the progression of CRPC."

sparser
"Circular RNA hsa_circ_0005185 functions as a molecular scaffold, facilitating the interaction between OTUB1 and RAB8A, leading to the deubiquitination of RAB8A. This process promotes primary cilia formation and enhances GLI3R production in the Hedgehog signaling pathway, ultimately inhibiting androgen receptor activity and suppressing the progression of prostate cancer."

sparser
"OTUB1 is known to be critical in various cellular processes, including DNA damage response, apoptosis, proliferation, and cancer development. [ xref , xref , xref ] However, the potential interaction between OTUB1 and RAB8A and the mechanism by which OTUB1 promotes RAB8A deubiquitination have not been reported."

sparser
"Circ_0005185 Binds to the 196–247 aa Region of OTUB1 and the 32–83 aa Region of RAB8A."

sparser
"The mass spectrometry analysis revealed that circ_0005185 can bind to OTUB1 and RAB8A when compared to the control group."

reach
"The Co‐IP results demonstrated that OTUB1 can bind to RAB8A and that the overexpression of circ_0 005185 enhances this interaction."

sparser
"We also assessed the effect of circ_0 005185 on the binding of OTUB1 to RAB8A. Co‐IP analysis indicated that the overexpression of circ_0 005185 enhanced the binding of OTUB1 to RAB8A (Figure  xref )."

sparser
"To validate the binding of the OTUB1 and RAB8A proteins to circ_0005185, we performed RIP experiments."

sparser
"Nonspecific results were excluded using western blotting, which demonstrated successful binding of the OTUB1 and RAB8A antibodies to magnetic beads (Figure  xref ), suggesting a binding relationship between circ_0005185, OTUB1, and RAB8A. Next, we used the CatRAPID database to predict specific regions of interaction between RAB8A and OTUB1 with circ_0005185."

sparser
"These findings suggest that circ_0 005185 interacts specifically with the 196–247 aa region of OTUB1 and the 32–83 aa region of RAB8A, highlighting their potential roles in mediating the effects of circ_0 005185 on prostate cancer progression."

sparser
"circ_0005185 Facilitates the Deubiquitination at K48 Site of RAB8A by Mediating the Interaction Between OTUB1 and RAB8A."

sparser
"Next, a Co‐IP assay was conducted to examine the potential interaction between OTUB1 and RAB8A. The results revealed that RAB8A was successfully detected by western blotting using an OTUB1 antibody along with magnetic beads to isolate the bound proteins (Figure  xref )."

sparser
"Collectively, these results suggest that circ_0 005185 mediates the interaction between OTUB1 and RAB8A and promotes the deubiquitination of RAB8A. This process inhibits the degradation of RAB8A and increases its protein levels, highlighting the regulatory role of circ_0 005185 in this pathway."

reach
"21 , 22 , 23 However, the potential interaction between OTUB1 and RAB8A and the mechanism by which OTUB1 promotes RAB8A deubiquitination have not been reported.2 Results."

reach
"Next, we used the CatRAPID database to predict specific regions of interaction between RAB8A and OTUB1 with circ_0005185."

reach
"We also assessed the effect of circ_0 005185 on the binding of OTUB1 to RAB8A."

reach
"Co‐IP analysis indicated that the overexpression of circ_0 005185 enhanced the binding of OTUB1 to RAB8A (Figure 4B)."

reach
"Collectively, these results suggest that circ_0 005185 mediates the interaction between OTUB1 and RAB8A and promotes the deubiquitination of RAB8A."

reach
"32 , 33 However, the interaction between OTUB1 and RAB8A in prostate cancer cells, and the role of circRNAs in this context, has not been reported."