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Figure 6


Fig. 6. (A) Yeast two-hybrid analysis of interaction of Lasp-1 with palladin. (i) Schematic representations of constructs used for the yeast two-hybrid analysis. (ii) The strength of the interaction between bait and prey constructs, as indicated by cell growth and ß-galactosidase activity was scaled from no interaction (-) to strong interaction (+++). Yeast two-hybrid analysis indicates that Lasp-1 interacts through its SH3 domain with the poly-proline motif in the 140 kDa isoform, but not that in the 90 kDa isoform. A mutation to the putative poly-proline motif abrogates this interaction in the 140 kDa isoform. (B) HeLa cells express both the 140 kDa and 90 kDa isoforms of palladin. The SH3 domain of Lasp-1 co-precipitates the 140 kDa palladin. GST protein or the GST domain fused to the SH3 domain of Lasp-1 was incubated with HeLa-cell lysate and precipitated with glutathione Sepharose. Western blot analysis indicates that the SH3 domain of Lasp-1 specifically co-precipitates the 140 kDa isoform but not the 90 kDa isoform of palladin (lane, GST-SH3 bound).





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