Results 11 to 20 of about 14,978 (204)

Dynactin Is Necessary for Synapse Stabilization [PDF]

open access: yesNeuron, 2002
We present evidence that synapse retraction occurs during normal synaptic growth at the Drosophila neuromuscular junction (NMJ). An RNAi-based screen to identify the molecular mechanisms that regulate synapse retraction identified Arp-1/centractin, a subunit of the dynactin complex.
Eaton, Benjamin A   +2 more
openaire   +2 more sources

Microtubule Motors: Doin’ It without Dynactin [PDF]

open access: yesCurrent Biology, 2013
The minus-end directed microtubule motor protein cytoplasmic dynein contributes to many aspects of cell division and it is generally believed that these mitotic functions require the dynein activator and processivity factor, dynactin. New research now shows that dynein accomplishes many of its mitotic functions without dynactin.
Wadsworth, Patricia, Lee, Wei-Lih
openaire   +2 more sources

Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS–Hook–FHIP complexes

open access: yeseLife, 2021
In eukaryotic cells, intracellular components are organized by the microtubule motors cytoplasmic dynein-1 (dynein) and kinesins, which are linked to cargos via adaptor proteins.
Jenna R Christensen   +6 more
doaj   +1 more source

Dynein-dynactin complex is essential for dendritic restriction of TM1-containing Drosophila Dscam. [PDF]

open access: yesPLoS ONE, 2008
BACKGROUND:Many membrane proteins, including Drosophila Dscam, are enriched in dendrites or axons within neurons. However, little is known about how the differential distribution is established and maintained.
Jacob Shun-Jen Yang   +2 more
doaj   +1 more source

Dynamic recruitment of CDK5RAP2 to centrosomes requires its association with dynein. [PDF]

open access: yesPLoS ONE, 2013
CDK5RAP2 is a centrosomal protein known to be involved in the regulation of the γ-tubulin ring complex and thus the organization of microtubule arrays. However, the mechanism by which CDK5RAP2 is itself recruited to centrosomes is poorly understood.
Yue Jia   +4 more
doaj   +1 more source

p25 of the dynactin complex plays a dual role in cargo binding and dynactin regulation [PDF]

open access: yesJournal of Biological Chemistry, 2018
Cytoplasmic dynein binds its cargoes via the dynactin complex and cargo adapters, and the dynactin pointed-end protein p25 is required for dynein-dynactin binding to the early endosomal dynein adapter HookA (Hook in the fungus Aspergillus nidulans). However, it is unclear whether the HookA-dynein-dynactin interaction requires p27, another pointed-end ...
Rongde, Qiu, Jun, Zhang, Xin, Xiang
openaire   +2 more sources

Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein

open access: yesBMC Evolutionary Biology, 2012
Background Dynactin is a large multisubunit protein complex that enhances the processivity of cytoplasmic dynein and acts as an adapter between dynein and the cargo.
Hammesfahr Björn, Kollmar Martin
doaj   +1 more source

Dynactin-dependent cortical dynein and spherical spindle shape correlate temporally with meiotic spindle rotation in Caenorhabditis elegans. [PDF]

open access: yes, 2015
Oocyte meiotic spindles orient with one pole juxtaposed to the cortex to facilitate extrusion of chromosomes into polar bodies. In Caenorhabditis elegans, these acentriolar spindles initially orient parallel to the cortex and then rotate to the ...
Andaya, Armann   +9 more
core   +1 more source

Huntingtin facilitates dynein/dynactin-mediated vesicle transport [PDF]

open access: yesProceedings of the National Academy of Sciences, 2007
Cytoplasmic dynein is a multisubunit microtubule motor complex that, together with its activator, dynactin, drives vesicular cargo toward the minus ends of microtubules. Huntingtin (Htt) is a vesicle-associated protein found in both neuronal and nonneuronal cells that is thought to be involved in vesicular transport.
Juliane P, Caviston   +4 more
openaire   +2 more sources

Structural basis for cytoplasmic dynein-1 regulation by Lis1

open access: yeseLife, 2022
The lissencephaly 1 gene, LIS1, is mutated in patients with the neurodevelopmental disease lissencephaly. The Lis1 protein is conserved from fungi to mammals and is a key regulator of cytoplasmic dynein-1, the major minus-end-directed microtubule motor ...
John P Gillies   +6 more
doaj   +1 more source

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