1. Identification of a third myosin-5a-melanophilin interaction that mediates the association of myosin-5a with melanosomes.
- Author
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Pan J, Zhou R, Yao LL, Zhang J, Zhang N, Cao QJ, Sun S, and Li XD
- Subjects
- Animals, Mice, Humans, Myosin Heavy Chains metabolism, Myosin Heavy Chains genetics, Melanocytes metabolism, Melanosomes metabolism, Myosin Type V metabolism, Myosin Type V genetics, Adaptor Proteins, Signal Transducing metabolism, Adaptor Proteins, Signal Transducing genetics, Protein Binding
- Abstract
Transport and localization of melanosome at the periphery region of melanocyte are depended on myosin-5a (Myo5a), which associates with melanosome by interacting with its adaptor protein melanophilin (Mlph). Mlph contains four functional regions, including Rab27a-binding domain, Myo5a GTD-binding motif (GTBM), Myo5a exon F-binding domain (EFBD), and actin-binding domain (ABD). The association of Myo5a with Mlph is known to be mediated by two specific interactions: the interaction between the exon-F-encoded region of Myo5a and Mlph-EFBD and that between Myo5a-GTD and Mlph-GTBM. Here, we identify a third interaction between Myo5a and Mlph, that is, the interaction between the exon-G-encoded region of Myo5a and Mlph-ABD. The exon-G/ABD interaction is independent from the exon-F/EFBD interaction and is required for the association of Myo5a with melanosome. Moreover, we demonstrate that Mlph-ABD interacts with either the exon-G or actin filament, but cannot interact with both of them simultaneously. Based on above findings, we propose a new model for the Mlph-mediated Myo5a transportation of melanosomes., Competing Interests: JP, RZ, LY, JZ, NZ, QC, SS, XL No competing interests declared, (© 2024, Pan et al.)
- Published
- 2024
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