Fig. 1. Mapping of EB1 and Mlph domains required for interaction. For A and B the left-hand part shows the relationship of truncated test proteins, indicated with solid lines, to the domain structures of EB1 (A) and Mlph (B). The right-hand part shows the results of the -galactosidase reporter gene assay for each test protein with either Mlph aa367-590 (A) or EB1 aa1-268 and MyoVa MSGTA (B). 1 and 2 denote the position of -helices in EB1; ABD, actin-binding domain; CC, coiled coil; CH, calponin homology domain; EFBD, MyoVa exon F binding domain; GTBD, MyoVa globular tail binding domain; MBD, MyoVa binding domain; SHD1, synaptotagmin homology domain; R27BD, Rab27a binding domain; ZnF, Zn²⁺ finger. Panel C is an alignment of part of Mlph and MyRIP sequences from human (Hs Mlph accession NP_077006.1 and Hs MyRIP accession BAC15555.1), mouse (Mm accession BAB41087.1), rat (Rn accession NP_001012135.1), chicken (Gg Mlph accession XP_421876.2) and zebrafish (Dr Mlpha accession NP_001073147.1 and Dr Mlphb accession XP_685065.2) showing the position of the Mlph IP motifs (red) and the coiled coil region (green). Alignment of sequences was conducted using Muscle protein multiple sequence alignment software available at http://phylogenomics.berkeley.edu/cgi-bin/muscle/input_muscle.py. Numbering indicates the amino acid position of each sequence.