Fig. 4.
Fig. 4. The guanine nucleotide exchange domain of C3G is involved in enhancement of cell adhesion. (A) Inducible expression of C3G or its mutant in 32D cells. A clone of 32D/EpoR-Wt cells transfected with pTet-C3G (32DE/Tet-C3G) or pTet-C3G-dSS (32DE/Tet-C3G-dSS), coding for C3G or its mutant lacking the guanine nucleotide exchange domain, respectively, was cultured for 24 hours with (+) or without (−) Tet, as indicated. TCL were extracted and subjected to anti-C3G immunoblotting. Positions of C3G and its mutant, C3G-dSS, are indicated. (B) 32DE/Tet-C3G and 32DE/Tet-C3G-dSS cells were cultured for 24 hours with (+) or without (−) Tet, as indicated, and subjected to the cell adhesion assay as described in Materials and Methods.

The guanine nucleotide exchange domain of C3G is involved in enhancement of cell adhesion. (A) Inducible expression of C3G or its mutant in 32D cells. A clone of 32D/EpoR-Wt cells transfected with pTet-C3G (32DE/Tet-C3G) or pTet-C3G-dSS (32DE/Tet-C3G-dSS), coding for C3G or its mutant lacking the guanine nucleotide exchange domain, respectively, was cultured for 24 hours with (+) or without (−) Tet, as indicated. TCL were extracted and subjected to anti-C3G immunoblotting. Positions of C3G and its mutant, C3G-dSS, are indicated. (B) 32DE/Tet-C3G and 32DE/Tet-C3G-dSS cells were cultured for 24 hours with (+) or without (−) Tet, as indicated, and subjected to the cell adhesion assay as described in Materials and Methods.

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