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- W1972769834 abstract "Myosin VI is one of 18 known classes of the molecular motor superfamily called myosin (1,2). All myosins rapidly bind and hydrolyze ATP in the presence or absence of actin. Until recently it was thought that all myosins moved toward the barbed (+) end of the actin filament. Myosin VI is the exception to that rule and may be unique among the myosin family members in that it moves toward the pointed (-) end of the actin filament (3).Our working model for myosin VI in a cell is that the full-length protein exists as a monomer if not bound to cargo. Binding of myosin VI monomers to cargo alters the conformation of the molecule, possibly exposing the high probability coiled-coil region (dimerization domain). Once dimerized, the myosin VI can move a vesicle processively toward the minus-end of an actin filament. GiPC and optineurin, two of the known myosin VI binding partners can dimerize, and thus potentially can initiate the dimerization of myosin VI when it binds.Both GiPC and optineurin has been expressed in insect Sf9 cells. Surface plasmon resonance (SPR) analysis showed that both GiPC and optineurin interact with full-length myosin VI within the nanomolar range. Both GiPC and optineurin when incubated with full-length myosin VI initiated its dimerization showed by ATPase assays, EM and TIRF microscopy.[1] Mermall V, Post PL, Mooseker MS. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:527-33, 1998.[2] Sellers JR, Goodson HV: Motor proteins 2: myosins. Protein Profile 2:1323-1423, 1995.[3] Wells AL, Lin AW, Chen LQ, Safer D, Cain SM, Hasson T, Carragher BO, Milligan RA, Sweeney HL. Myosin VI is an actin-based motor that moves backwards. Nature. 401:505-8, 1999." @default.
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- W1972769834 date "2009-02-01" @default.
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- W1972769834 title "Cargo-mediated dimerization of Myosin VI" @default.
- W1972769834 doi "https://doi.org/10.1016/j.bpj.2008.12.3877" @default.
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