A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein

@article{Gleave2014ASA,
  title={A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein},
  author={E. Gleave and H. Schmidt and A. Carter},
  journal={Journal of Structural Biology},
  year={2014},
  volume={186},
  pages={367 - 375}
}
  • E. Gleave, H. Schmidt, A. Carter
  • Published 2014
  • Biology, Medicine
  • Journal of Structural Biology
    • Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor… CONTINUE READING
    View on PubMed
    doi.org
    16 Citations
    Background Citations
    9
    Methods Citations
    1
    16 Citations
    Citation Type

    Citation Type

    Review: Structure and mechanism of the dynein motor ATPase
    • 57
    Structure of human cytoplasmic dynein-2 primed for its powerstroke
    • 131
    • PDF
    Dynein motors: How AAA+ ring opening and closing coordinates microtubule binding and linker movement
    • H. Schmidt
    • Biology, Medicine
    • BioEssays : news and reviews in molecular, cellular and developmental biology
    • 2015
    • 25
    Mechanisms of Regulation of Cytoplasmic Dynein
    Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein
    • 51
    • PDF
    Lis1 has two opposing modes of regulating cytoplasmic dynein
    • PDF
    Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.
    • 42
    A physical model describing the transport mechanisms of cytoplasmic dynein
    • PDF
    Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate
    • 97
    • PDF
    AAA+ ATPases: structural insertions under the magnifying glass.

    References

    SHOWING 1-10 OF 65 REFERENCES
    Crystal Structure of the Dynein Motor Domain
    • 234
    • PDF
    The 2.8-Å Crystal Structure of the Dynein Motor Domain
    • 55
    • Highly Influential
    Insights into dynein motor domain function from a 3.3 Å crystal structure
    • 152
    • PDF
    X-ray structure of a functional full-length dynein motor domain
    • 108
    • PDF
    ATP-Driven Remodeling of the Linker Domain in the Dynein Motor
    • 79
    • PDF
    An extended microtubule-binding structure within the dynein motor domain
    • 294
    Crystal clear insights into how the dynein motor moves
    • A. Carter
    • Biology, Medicine
    • Journal of Cell Science
    • 2013
    • 77
    • PDF
    Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein.
    • 219
    The 2.8 Å crystal structure of the dynein motor domain
    • 163
    • Highly Influential
    Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor
    • 200
    • PDF