8ARD
Myosin VI proximal tail domain, dimeric
Summary for 8ARD
| Entry DOI | 10.2210/pdb8ard/pdb |
| Descriptor | Unconventional myosin-VI (2 entities in total) |
| Functional Keywords | dimer, myosin vi, myo6, motor protein |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 8244.52 |
| Authors | Kikuti, C.M.,Sirkia, H.,Houdusse, A. (deposition date: 2022-08-16, release date: 2023-08-30, Last modification date: 2024-03-13) |
| Primary citation | Canon, L.,Kikuti, C.,Planelles-Herrero, V.J.,Lin, T.,Mayeux, F.,Sirkia, H.,Lee, Y.I.,Heidsieck, L.,Velikovsky, L.,David, A.,Liu, X.,Moussaoui, D.,Forest, E.,Hook, P.,Petersen, K.J.,Morgan, T.E.,Di Cicco, A.,Sires-Campos, J.,Derivery, E.,Levy, D.,Delevoye, C.,Sweeney, H.L.,Houdusse, A. How myosin VI traps its off-state, is activated and dimerizes. Nat Commun, 14:6732-6732, 2023 Cited by PubMed Abstract: Myosin VI (Myo6) is the only minus-end directed nanomotor on actin, allowing it to uniquely contribute to numerous cellular functions. As for other nanomotors, the proper functioning of Myo6 relies on precise spatiotemporal control of motor activity via a poorly defined off-state and interactions with partners. Our structural, functional, and cellular studies reveal key features of myosin regulation and indicate that not all partners can activate Myo6. TOM1 and Dab2 cannot bind the off-state, while GIPC1 binds Myo6, releases its auto-inhibition and triggers proximal dimerization. Myo6 partners thus differentially recruit Myo6. We solved a crystal structure of the proximal dimerization domain, and show that its disruption compromises endocytosis in HeLa cells, emphasizing the importance of Myo6 dimerization. Finally, we show that the L926Q deafness mutation disrupts Myo6 auto-inhibition and indirectly impairs proximal dimerization. Our study thus demonstrates the importance of partners in the control of Myo6 auto-inhibition, localization, and activation. PubMed: 37872146DOI: 10.1038/s41467-023-42376-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.219 Å) |
Structure validation
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