Fig. 2

Genomic structure of the mouse epb4.1l5 locus and expression of its two major splice isoforms. (A) Diagram of the inton/exon structure of the Mus musculus epb4.1l5 locus. Exons that are common to both isoforms are black, the exons unique to epb4.1l5^long are indicated in red and the unique exon in epb4.1l5^short is indicated in green. Bars represent 1 kb and 10 kb scales for exon and intron lengths, respectively. (B) ClustalX alignment of mouse Epb4.1l5^long and zebrafish Moe. Ymo1^long and Moe share a high degree of homology within the FERM domain (black). Ymo1^long and Ymo1^short are identical up to Lysine 444 (blue arrow) and then alternately spliced into the long (red) and short (green) isoforms. Moe and Epb4.1l5^long, and Epb4.1l5^short have predicted C′terminal PDZ-binding domains (Pink [TTEL]) and (light green [MTEI]). (*) identical, (:) highly conserved, (.) Moe and Epb4.1l5^long, and Epb4.1l5^short have predicted C′terminal PDZ-binding domains (Pink moderately conserved. (C) Western analysis of mouse tissues with antibodies raised against the unique C′terminal sequences of Epb4.1l5^long and Epb4.1l5^short. Two bands are immunoreactive with the anti-Epb4.1l5^long antibody, one migrates at the expected molecular weight of Epb4.1l5^long (100 kDa) and is present in the eye, brain, heart, lung, kidney, and testis. An additional band migrates at 75 kDa, which is probably non-specific. Two bands are recognized by the affinity purified Epb4.1l5^short antibody. A lower band migrates at the predicted molecular weight of 56 kDa and is present in brain, liver, lung, kidney, pancreas, and gut. A second band with a broad expression pattern migrates at approximately 75 kDa. Anti-α-Tubulin was used as a loading control.