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Figure 1


Fig. 1. RET interacts with SH2-Bß in a two-hybrid screen. (A) Schematic representation of the pGilda-RETIC bait. Cad, Cadherin domain; Cys, cysteine-rich domain; TM, transmembrane domain; TK, tyrosine kinase domain; LexA, LexA fusion vector pGilda. (B) The human SH2-Bß region (amino acids 498-670) containing the SH2 domain was isolated from the two-hybrid screen. PH, pleckstrin homology domain; SH2, Src homology 2 domain. (C,D) Filter assay and liquid culture assay using o-nitrophenyl-D-galactoside (ONPG) was performed for ß-galactosidase activity analysis. Full-length wild-type SH2-Bß was co-transformed into yeast reporter strain EGY48 with the bait encoding the intracellular domain of RET, TrkA or EGF receptor. To determine the binding domain of the interaction between SH2-Bß and RET, RETIC bait was transformed with the SH2 domain, the PH domain of SH2-Bß or R555E (SH2-Bß dominant-negative mutant). Positive and negative controls are described in Materials and Methods.





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