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. 2016 Aug 26;291(43):22373–22385. doi: 10.1074/jbc.M116.730689

FIGURE 1.

FIGURE 1.

Myosin 10 constructs. A, diagram showing each of the constructs used in experiments to determine how different domains contribute to M10 behavior in cells. Numbers shown below each diagram refer to amino acid residue numbers. B shows the sequence of the SAH domain and anti-parallel coiled-coil domain, indicating which regions are deleted in M10-Δ1 and M10-Δ2. Residues 813–909 have been shown to form an SAH domain in vitro, whereas residues 885–913 have been shown to form an anti-parallel CC in vitro. In M10-Δ1, the entire SAH/CC sequence (815–938) is deleted. In M10-Δ2, only the last 86 residues (852–938) from this region are deleted. This deletes the CC and the distal part of the SAH domain, leaving the EKR-rich region of the SAH domain intact. Also indicated are the truncations investigated in two earlier cell biological studies, where the distal part of the SAH domain and the anti-parallel coiled-coil region were both deleted and replaced with either the coiled-coil forming region from myosin 5a (M5CC) or a GCN4 zipper motif.