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. 1998 Apr 1;18(7):2360–2369. doi: 10.1523/JNEUROSCI.18-07-02360.1998

Fig. 1.

Fig. 1.

A, Interaction trap selection for dSLIP1. dSLIP1 was introduced into EGY195 containing the indicated bait plasmids. The plate on the left shows that in the presence of glucose and leucine all combinations permit growth, whereas the plate on the right shows that only the combination of dSLIP1 with dSlo-C665–1164 survives in the presence of galactose and the absence of leucine. dSlo-C665–1164, the C-terminal 499 amino acids of dSlo; dSlo-N1–127, the N-terminal 127 amino acids of dSlo;rKir3.4-C103–417, the C-terminal 314 amino acids of Kir3.4 (Krapivinsky et al., 1995a,b). B, Full-length coding sequence of dSLIP1. The domain recovered in the original interaction trap screen started from amino acid 101 and extended through the coding region; potential substrate sites for serine/threonine protein kinases are denoted byasterisks. The domain of dSLIP1 with homology to the PDZ domain of α1 syntrophin is overlined.C, The dSLIP1 cDNA encodes the full-length protein. Bacterially expressed dSLIP1 (His–tag fusion protein; lane 1), in vitro translated dSLIP1 (lane 2), and Drosophila embryo proteins (lane 3) were prepared as a Western blot and probed with a polyclonal antiserum directed against recombinant dSLIP1. The dSLIP1 antiserum detected bands of similar molecular weights.