IndraLab

Statements

VHL binds USP33. 16 / 16
6 1 | 4 5
biogrid
No evidence text available
19706539
sparser
"The USP33-VHL interaction may have clinical significance because naturally occurring mutations that have been found in the beta-domain of USP33 disrupt the interaction between the two proteins."
18687060
sparser
"The proteasome has both ubiquitin ligases and DUBs that associate with it (Crosas et al., 2006) , and several DUB-ligase pairs interact directly, including BRCC36-BRCA1, BAP1-BRCA1, USP4-Ro52, USP7-MDM2, USP8-GRAIL, USP20-pVHL, USP33-pVHL and USP44-APC (Kee and Huibregtse, 2007; Marfany and Denuc, 2008; Ventii and Wilkinson, 2008) ."
19571111
biogrid
No evidence text available
19706539
biogrid
No evidence text available
11739384
reach
"Further investigations are warranted to probe the biochemical and biological functions of the interaction between pVHL and VDU1 and VDU2 and to dissect functional and physiological differences between[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12056827
hprd
No evidence text available
11739384
reach
"Together, our results suggest that VDU1 and VDU2 might be relevent to pVHL related tumorigenesis.In conclusion, our previously published results and current data indicate that the interaction between [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12056827
reach
"Finally, we demonstrate that VDU1 is able to be ubiquitinated via a pVHL dependent pathway for proteasomal degradation, and VHL mutations that disrupt the interaction between VDU1 and pVHL abrogate the ubiquitination of VDU1."
11739384
biogrid
No evidence text available
11739384
sparser
"We propose a model, in which hSP56 may function as a novel regulator of ubiquitination-dependent protein degradation pathways by altering the enzymatic activity of VDU1 or by regulating the interactio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19118533
biogrid
No evidence text available
11739384
sparser
"Finally, we demonstrate that VDU1 is able to be ubiquitinated via a pVHL-dependent pathway for proteasomal degradation, and VHL mutations that disrupt the interaction between VDU1 and pVHL abrogate the ubiquitination of VDU1."
11739384
reach
"In the current studies and together with our previous report [30], we have demonstrated that both VDU1 and VDU2 also bind to the beta-domain of pVHL and several naturally occurring mutations in the be[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12056827
biogrid
No evidence text available
11739384
sparser
"We have determined that the VDU1-interacting region in pVHL is located in its beta-domain, and several naturally occurring mutations located in this domain disrupt the interaction between pVHL and VDU1 protein."
11739384