Results 31 to 40 of about 9,677 (245)
Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin
Journal of Cell Biology, 2022 d’Amico et al. report a structure-function analysis of Spindly, a Dynein–Dynactin adaptor that functions at kinetochores during mitosis. They propose that Spindly is auto-inhibited. Its binding to two distinct kinetochore triggers, the RZZ complex and an
Ennio A d'Amico +12 more
semanticscholar +1 more source
Dynactin is required for bidirectional organelle transport [PDF]
The 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.
Anna S. Serpinskaya +6 more
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TRAPPC9 mediates the interaction between p150 and COPII vesicles at the target membrane. [PDF]
PLoS ONE, 2012 The transport of endoplasmic reticulum (ER)-derived COPII vesicles toward the ER-Golgi intermediate compartment (ERGIC) requires cytoplasmic dynein and is dependent on microtubules. p150(Glued), a subunit of dynactin, has been implicated in the transport
Min Zong +7 more
doaj +1 more source
Mechanism of Dynamitin-mediated Disruption of Dynactin [PDF]
Journal 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 ...
Michael E. Rodgers +4 more
openaire +3 more sources
eLife, 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
Structure of dynein-dynactin on microtubules shows tandem recruitment of cargo adaptors
bioRxiv, 2022 Cytoplasmic dynein is a microtubule motor that is activated by its cofactor dynactin and a coiled-coil cargo adaptor. There is currently limited structural information on how the resulting complex interacts with microtubules and how adaptors are ...
Sami Chaaban, A. Carter
semanticscholar +1 more source
Dynein-dynactin complex is essential for dendritic restriction of TM1-containing Drosophila Dscam. [PDF]
PLoS 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
Structural basis for cytoplasmic dynein-1 regulation by Lis1
eLife, 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]
Traffic, 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
Trina A. Schroer, Matthew A. Berezuk
openaire +3 more sources
Dynamic recruitment of CDK5RAP2 to centrosomes requires its association with dynein. [PDF]
PLoS 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