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. 2015 Jul 16;5:12230. doi: 10.1038/srep12230

Figure 5. The interaction of A3G and PTEN depends on the binding domain.

Figure 5

(A) The binding capacity of A3G and PTEN is related to a zinc-coordinating domain of A3G but not to its phosphorylation state. PTEN was co-immunoprecipitated from 293T cells transfected with different A3G mutants (T32A, T32D, T32E, T218A, T218D, T218E, T32A/T218A, T32A/T218D, T32D/T218A and T32DT218D) and A3G CD mutant plasmids (CD2-1 and CD2–2). PTEN was not co-immunoprecipitated from 293T cells transfected with the A3G CD mutant plasmid CD1-1. All data are repeated for three times in the same condition. (B) Binding domain of PTEN. Shown is an illustration of the PTEN binding domain. (C) Binding capacity is related to the domain of PTEN. The top image shows that A3G HA-tagged protein was co-immunoprecipitated from 293T cells co-transfected with A3G HA-tagged plasmid and PTEN Myc-tagged CD mutant plasmids (CD1CD2, CD3) but not with PTEN CD1 mutant plasmid. The bottom image shows the input of 293T cells co-transfected with A3G HA-tagged plasmid and PTEN Myc-tagged CD mutant plasmids. All data are repeated for three times in the same condition.