Results 11 to 20 of about 8,973 (210)
Dynactin has two antagonistic regulatory domains and exerts opposing effects on dynein motility. [PDF]
PLoS ONE, 2017 Dynactin is a dynein-regulating protein that increases the processivity of dynein movement on microtubules. Recent studies have shown that a tripartite complex of dynein-dynactin-Bicaudal D2 is essential for highly processive movement.
Takuya Kobayashi +3 more
doaj +3 more sources
Dynactin Is Necessary for Synapse Stabilization [PDF]
Neuron, 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 +3 more sources
Microtubule Motors: Doin’ It without Dynactin [PDF]
Current 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 +3 more sources
Human dynein-dynactin is a fast processive motor in living cells. [PDF]
ElifeMinus-end directed transport along microtubules in eukaryotes is primarily mediated by cytoplasmic dynein and its cofactor dynactin. Significant advances have been made in recent years characterizing human dynein–dynactin structure and function using in ...
Verma V, Wadsworth P, Maresca TJ.
europepmc +2 more sources
Dynactin Is Required for Microtubule Anchoring at Centrosomes [PDF]
The Journal of Cell Biology, 1999 The multiprotein complex, dynactin, is an integral part of the cytoplasmic dynein motor and is required for dynein-based motility in vitro and in vivo. In living cells, perturbation of the dynein–dynactin interaction profoundly blocks mitotic spindle assembly, and inhibition or depletion of dynein or dynactin from meiotic or mitotic cell extracts ...
N J, Quintyne +5 more
openaire +4 more sources
dnc-1/dynactin 1 knockdown disrupts transport of autophagosomes and induces motor neuron degeneration. [PDF]
PLoS ONE, 2013 Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the progressive loss of motor neurons. We previously showed that the expression of dynactin 1, an axon motor protein regulating retrograde transport, is markedly ...
Kensuke Ikenaka +11 more
doaj +3 more sources
The Long Haul: Microtubule Motors as the Essential Supply Line for Neuronal Longevity. [PDF]
J NeurochemTo survive a lifetime, neurons depend on a high‐fidelity logistics network powered by microtubule motors. We explore how a broad spectrum of genetic defects in this machinery drive a devastating spectrum of neurodevelopmental and neurodegenerative diseases, including Hereditary Spastic Paraplegia (HSP), Charcot–Marie‐Tooth Type 2 (CMT2), and ...
Turner ED, Twelvetrees AE.
europepmc +2 more sources
Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein [PDF]
BMC 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 +2 more sources
Interaction of tau protein with the dynactin complex [PDF]
The EMBO Journal, 2007 Tau is an axonal microtubule-associated protein involved in microtubule assembly and stabilization. Mutations in Tau cause frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), and tau aggregates are present in Alzheimer's disease and other tauopathies.
Enrico, Magnani +8 more
openaire +3 more sources
NuMA and Ninein: Dynein Cargo-Adaptors Without a Classical Cargo. [PDF]
CellsDynein is a minus-end-directed microtubule motor that transports a variety of cargoes. Cargo specificity is mediated by a class of adaptor proteins that bind to the interface between dynein and dynactin, along the length of the Arp1 filament of dynactin,
Guo K, Merdes A.
europepmc +2 more sources