New insights into the mechanism of dynein motor regulation by lissencephaly-1
Lissencephaly (‘smooth brain’) is a severe brain disease associated with numerous symptoms, including cognitive impairment, and shortened lifespan. The main causative gene of this disease – lissencephaly-1 (LIS1) – has been a focus of intense scrutiny ...
Steven M Markus +2 more
doaj +1 more source
Mutant dynactin in motor neuron disease [PDF]
Impaired axonal transport in motor neurons has been proposed as a mechanism for neuronal degeneration in motor neuron disease. Here we show linkage of a lower motor neuron disease to a region of 4 Mb at chromosome 2p13. Mutation analysis of a gene in this interval that encodes the largest subunit of the axonal transport protein dynactin showed a single
Imke, Puls +12 more
openaire +2 more sources
Characterization of the p22 Subunit of Dynactin Reveals the Localization of Cytoplasmic Dynein and Dynactin to the Midbody of Dividing Cells [PDF]
Dynactin, a multisubunit complex that binds to the microtubule motor cytoplasmic dynein, may provide a link between dynein and its cargo. Many subunits of dynactin have been characterized, elucidating the multifunctional nature of this complex. Using a dynein affinity column, p22, the smallest dynactin subunit, was isolated and microsequenced.
S, Karki, B, LaMonte, E L, Holzbaur
openaire +2 more sources
ZW10 Helps Recruit Dynactin and Dynein to the Kinetochore [PDF]
Mutations in the Drosophila melanogaster zw10 gene, which encodes a conserved, essential kinetochore component, abolish the ability of dynein to localize to kinetochores. Several similarities between the behavior of ZW10 protein and dynein further support a role for ZW10 in the recruitment of dynein to the kinetochore: (a) in response to bipolar ...
Starr, Daniel A +3 more
openaire +4 more sources
Functional coupling of microtubules to membranes - implications for membrane structure and dynamics [PDF]
The microtubule network dictates much of the spatial patterning of the cytoplasm, and the coupling of microtubules to membranes controls the structure and positioning of organelles and directs membrane trafficking between them.
Stephens, David J
core +1 more source
Lis1 activates dynein motility by modulating its pairing with dynactin [PDF]
Lissencephaly-1 (Lis1) is a key cofactor for dynein-mediated intracellular transport towards the minus-ends of microtubules. It remains unclear whether Lis1 serves as an inhibitor or an activator of mammalian dynein motility.
Sara Volz +11 more
core +1 more source
Dynein and dynactin schematic.
A. Dynein and dynactin macromolecular complex organization. Both complexes are drawn approximately to scale from EM reconstruction images. B. Schematic of domain structure and binding sites of both the dynein intermediate chain isoform 2C and dynactin ...
Shangjin Sun (399678) +8 more
core +1 more source
Alpha-E-catenin binds to dynamitin and regulates dynactin-mediated intracellular traffic. [PDF]
Alpha-epithelial catenin (E-catenin) is an important cell-cell adhesion protein. In this study, we show that alpha-E-catenin also regulates intracellular traffic by binding to the dynactin complex component dynamitin.
Valeri Vasioukhin +5 more
core +1 more source
Analysis of the Dynein-Dynactin Interaction In Vitro and In Vivo [PDF]
Cytoplasmic dynein and dynactin are megadalton-sized multisubunit molecules that function together as a cytoskeletal motor. In the present study, we explore the mechanism of dynein-dynactin binding in vitro and then extend our findings to an in vivo context.
Stephen J, King +4 more
openaire +2 more sources
Kazrin is an endosomal adaptor for dynein/dynactin [PDF]
Abstract Kazrin is a protein widely expressed in vertebrates whose depletion causes a myriad of developmental defects, in part derived from altered cell adhesion, impaired cell migration and failure to undergo Epidermal to Mesenchymal Transition (EMT).
Ines Hernandez-Perez +6 more
openaire +1 more source

