IndraLab

Statements

VHL binds USP33. 12 / 19
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"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
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"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
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"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
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"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
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
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"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
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
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
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"Interestingly, several naturally occurring mutations in the VDU-binding domain of pVHL were found to disrupt the interaction between VDU1/VDU2 and pVHL, thus suggesting a functional relevance in pVHL-[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17961905
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"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
sparser
"Some of the disease-causing mutations in pVHL disrupt binding of USP33 to pVHL, underscoring the importance of these enzymes."
40061651
reach
"Some of the disease-causing mutations in pVHL disrupt binding of USP33 to pVHL, underscoring the importance of these enzymes."
40061651