A new direction for myosin

Rodriguez, Olga; Cheney, Richard E.

doi:10.1016/s0962-8924(00)01797-9

Cited by 15 publications

(8 citation statements)

References 35 publications

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“…Such a strong motor/cargo interaction is somewhat odd, considering the reversible cargo loading and unloading processes required for motor-mediated cargo transport. With such strong binding affinity, it would be difficult for myosin VI-bound Dab2 to dissociate from the motor, given that cellular concentrations of both myosin VI and Dab2 are quite high (Fazili et al, 1999;Hasson and Mooseker, 1994;Rodriguez and Cheney, 2000). It is possible and logically necessary that myosin VI employs some sort of regulatory switch to regulate Dab2-containing cargo loading and unloading.…”

Section: Discussionmentioning

confidence: 99%

Myosin VI Undergoes Cargo-Mediated Dimerization

Feng

Wei

et al. 2009

Cell

122

130

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Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.

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Section: Discussionmentioning

confidence: 99%

Myosin VI Undergoes Cargo-Mediated Dimerization

Feng

Wei

et al. 2009

Cell

122

130

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“…Myosins I and V move towards the barbed/plus end of the actin filaments, while myosin VI moves in the opposite direction [94,95]. Most processive cytoplasmic kinesins move toward the plus end of the microtubule with the exception of members of the kinesin-14 group.…”

Section: Alphaherpesviruses and The Host Cell Cytoskeleton: Interactimentioning

confidence: 99%

Alphaherpesviruses and the Cytoskeleton in Neuronal Infections

Zaichick

Bohannon

Smith

2011

Viruses

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Following infection of exposed peripheral tissues, neurotropic alphaherpesviruses invade nerve endings and deposit their DNA genomes into the nuclei of neurons resident in ganglia of the peripheral nervous system. The end result of these events is the establishment of a life-long latent infection. Neuroinvasion typically requires efficient viral transmission through a polarized epithelium followed by long-distance transport through the viscous axoplasm. These events are mediated by the recruitment of the cellular microtubule motor proteins to the intracellular viral particle and by alterations to the cytoskeletal architecture. The focus of this review is the interplay between neurotropic herpesviruses and the cytoskeleton.

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“…Thus, myosin VI may be involved in sorting cell components in a manner distinct from all other myosins. Current evidence suggests that it has roles both in particle transport and in pulling membranes down along polarized actin filaments [9,10].…”

Section: Introductionmentioning

confidence: 99%