Results 31 to 40 of about 8,973 (210)

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

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

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

Lissencephaly-1 promotes the recruitment of dynein and dynactin to transported mRNAs [PDF]

open access: yes, 2013
Microtubule-based transport mediates the sorting and dispersal of many cellular components and pathogens. However, the mechanisms by which motor complexes are recruited to and regulated on different cargos remain poorly understood.
Beat Suter   +15 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

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

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

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

Spindly is required for rapid migration of human cells

open access: yesBiology Open, 2018
Dynein is the sole processive minus-end-directed microtubule motor found in animals. It has roles in cell division, membrane trafficking, and cell migration.
Claudia Conte   +3 more
doaj   +1 more source

Regulation of mitochondria-dynactin interaction and mitochondrial retrograde transport in axons

open access: yeseLife, 2017
Mitochondrial transport in axons is critical for neural circuit health and function. While several proteins have been found that modulate bidirectional mitochondrial motility, factors that regulate unidirectional mitochondrial transport have been harder ...
Catherine M Drerup   +3 more
doaj   +1 more source

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