Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Characterization of RhoBTB-dependent Cul3 ubiquitin ligase complexes--evidence for an autoregulatory mechanism.

Berthold J, Schenkova K, Ramos S, Miura Y, Furukawa M, Aspenstroem P, Rivero F

RhoBTB proteins are atypical members of the Rho family of small GTPases. Two of the three RhoBTB proteins, RhoBTB1 and RhoBTB2, have been proposed as tumor suppressors and might function as adaptors of Cul3-dependent ubiquitin ligase complexes. Using yeast two-hybrid analysis and co-immunoprecipitation we show that all three RhoBTB proteins interact with Cul3. The interaction requires the N-terminal region of ... [more]

Exp. Cell Res. Nov. 15, 2008; 314(19);3453-65 [Pubmed: 18835386]

Throughput

  • Low Throughput

Additional Notes

  • Data not shown

Curated By

  • BioGRID