Fig. 1

Mitochondrial localization of the cell adhesion molecule 1 intracellular domain (C-ICD) peptide in lung epithelial cell lines. a Full-length amino acid sequences of the α-C-terminal fragment (αCTF) and the αC-terminal fragment mutant (αCTFmut) of cell adhesion molecule 1. The C-ICD and the cell adhesion molecule 1 intracellular domain mutant (C-ICDmut) are shown in the boxed portions. The arrow indicates the γ-secretase cleavage site. Dots indicate the amino acid residues as above. The 7-amino acid substitution and the 2-amino acid deletion in C-ICDmut are shown in italics and –, respectively. The structural motifs are underlined. TM, transmembrane domain; P4.1-IS, protein 4.1 interaction sequence; PDZ-BM, PDZ type II domain-binding motif. Amino acid residues are numbered according to the NCBI database sequence (accession number, CCD32610). b The unlabeled and FITC-labeled C-ICD and C-ICDmut peptides were detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and by silver staining (left) or Western blotting of the gels using antibodies against cell adhesion molecule 1 (CADM1) (middle) or FITC (right). c NCI-H441 (upper) and RLE-6TN (lower) cells were introduced with the FITC-labeled C-ICD or C-ICDmut peptide and stained with Mitotracker. Green (FITC) and red (Mitotracker) fluorescent images were merged, as shown in the right panels. Bar = 10 μm