Results 51 to 60 of about 17,522 (280)

Dynactin is required for bidirectional organelle transport [PDF]

open access: yesThe Journal of Cell Biology, 2003
Kinesin II is a heterotrimeric plus end–directed microtubule motor responsible for the anterograde movement of organelles in various cell types. Despite substantial literature concerning the types of organelles that kinesin II transports, the question of how this motor associates with cargo organelles remains unanswered.
Deacon, Sean W.   +6 more
openaire   +2 more sources

The actin capping protein in Aspergillus nidulans enhances dynein function without significantly affecting Arp1 filament assembly

open access: yesScientific Reports, 2018
The minus-end-directed microtubule motor cytoplasmic dynein requires the dynactin complex for in vivo functions. The backbone of the vertebrate dynactin complex is the Arp1 (actin-related protein 1) mini-filament whose barbed end binds to the ...
Jun Zhang, Rongde Qiu, Xin Xiang
doaj   +1 more source

Defective axonal transport in motor neuron disease [PDF]

open access: yes, 2007
Several recent studies have highlighted the role of axonal transport in the pathogenesis of motor neuron diseases. Mutations in genes that control microtubule regulation and dynamics have been shown to cause motor neuron degeneration in mice and in a ...
Baas   +77 more
core   +1 more source

Mechanism of Dynamitin-mediated Disruption of Dynactin [PDF]

open access: yesJournal of Biological Chemistry, 2007
Dynamitin is a commonly used inhibitor of cytoplasmic dynein-based motility in living cells. Dynamitin does not inhibit dynein directly but instead acts by causing disassembly of dynactin, a multiprotein complex required for dynein-based movement. In dynactin, dynamitin is closely associated with the subunits p150(Glued) and p24, which together form ...
Karin A, Melkonian   +4 more
openaire   +2 more sources

On and off controls within dynein–dynactin on native cargoes

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2021
Significance The dynein–dynactin nanomotor is required for vastly diverse cellular functions, including cell division and cargo transport. Why dynactin interacts separately with the dynein motor and with microtubules is poorly understood and ...
Paulomi Sanghavi   +4 more
semanticscholar   +1 more source

Dynactin polices two-way organelle traffic [PDF]

open access: yesThe Journal of Cell Biology, 2003
How is the bidirectional motion of organelles controlled? In this issue, Deacon et al. (2003) reveal the unexpected finding that dynactin (previously known to control dynein-based motility) binds to kinesin II and regulates anterograde movement of Xenopus melanosomes.
openaire   +2 more sources

New insights into the mechanism of dynein motor regulation by lissencephaly-1

open access: yeseLife, 2020
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

Molecular mechanism of dynein-dynactin complex assembly by LIS1. [PDF]

open access: yesScience
Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor.
Singh K   +5 more
europepmc   +2 more sources

Dystonia and Optic Neuropathy: Expanded Phenotype of Dynactin 1 Related Neurodegeneration

open access: yesMovement Disorders Clinical Practice, 2022
Axonal transport is essential to provide nutrients to axons and nerve terminals and to clear up misfolded proteins to avoid the accumulation of toxic aggregates.
S. Mehta   +6 more
semanticscholar   +1 more source

Dynactin Enhances the Processivity of Kinesin‐2 [PDF]

open access: yesTraffic, 2006
Kinesin‐2 is a major microtubule‐based motor in most cell types. Its in vitro motile properties have been analyzed extensively and been found to differ considerably from kinesin‐1. Although recombinant kinesin‐2 heterodimers exhibit processive movement, the processivity of the native kinesin‐2 holoenzyme has never been evaluated. Kinesin‐2 can interact
Matthew A, Berezuk, Trina A, Schroer
openaire   +2 more sources

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