2N12
Solution structure of human Myosin VI isoform3 (1050-1131)
Summary for 2N12
| Entry DOI | 10.2210/pdb2n12/pdb |
| Related | 2N0Z 2N10 2N11 2N13 6E5N |
| NMR Information | BMRB: 25544 |
| Descriptor | Unconventional myosin-VI (1 entity in total) |
| Functional Keywords | motor protein, protein transport |
| Biological source | Homo sapiens (Human) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Isoform 3: Cytoplasmic vesicle, clathrin- coated vesicle membrane. Isoform 4: Cytoplasmic vesicle, clathrin- coated vesicle membrane: Q9UM54 |
| Total number of polymer chains | 1 |
| Total formula weight | 9580.19 |
| Authors | He, F.,Walters, K. (deposition date: 2015-03-20, release date: 2016-03-02, Last modification date: 2024-05-15) |
| Primary citation | Wollscheid, H.P.,Biancospino, M.,He, F.,Magistrati, E.,Molteni, E.,Lupia, M.,Soffientini, P.,Rottner, K.,Cavallaro, U.,Pozzoli, U.,Mapelli, M.,Walters, K.J.,Polo, S. Diverse functions of myosin VI elucidated by an isoform-specific alpha-helix domain. Nat.Struct.Mol.Biol., 23:300-308, 2016 Cited by PubMed Abstract: Myosin VI functions in endocytosis and cell motility. Alternative splicing of myosin VI mRNA generates two distinct isoform types, myosin VI(short) and myosin VI(long), which differ in the C-terminal region. Their physiological and pathological roles remain unknown. Here we identified an isoform-specific regulatory helix, named the α2-linker, that defines specific conformations and hence determines the target selectivity of human myosin VI. The presence of the α2-linker structurally defines a new clathrin-binding domain that is unique to myosin VI(long) and masks the known RRL interaction motif. This finding is relevant to ovarian cancer, in which alternative myosin VI splicing is aberrantly regulated, and exon skipping dictates cell addiction to myosin VI(short) in tumor-cell migration. The RRL interactor optineurin contributes to this process by selectively binding myosin VI(short). Thus, the α2-linker acts like a molecular switch that assigns myosin VI to distinct endocytic (myosin VI(long)) or migratory (myosin VI(short)) functional roles. PubMed: 26950368DOI: 10.1038/nsmb.3187 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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