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myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar proteins Unconventional myosin VI, also called Myo6, or unconventional myosin-6, is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, cancer metastasis, deafness, and retinal development, among others. For example, the GIPC1 (GAIP interacting protein, C-terminus 1) adaptor protein mediates endocytosis by tethering PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development and cargo protein of GIPC1, to myosin VI motor through a regulated oligomerization mechanism, forming a PlexinD1/GIPC/myosin VI complex. This model corresponds to the myosin VI ubiquitin-binding domain (MyUb) that binds to ubiquitin chains, especially those linked via K63, K11, and K29. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",