Results 1 to 10 of about 8,973 (210)

Dynein and dynactin leverage their bivalent character to form a high-affinity interaction. [PDF]

open access: yesPLoS ONE, 2013
Cytoplasmic dynein and dynactin participate in retrograde transport of organelles, checkpoint signaling and cell division. The principal subunits that mediate this interaction are the dynein intermediate chain (IC) and the dynactin p150(Glued); however ...
Amanda E Siglin   +8 more
doaj   +3 more sources

Dynactin knockdown leads to synuclein aggregation by blocking autophagy in a zebrafish model of Parkinson's disease

open access: yesBrazilian Journal of Medical and Biological Research
Axons of dopaminergic neurons projecting from substantia nigra to striatum are severely affected in the early stage of Parkinson's disease (PD), with axonal degeneration preceding the loss of cell bodies.
Yongmei Wu   +14 more
doaj   +2 more sources

A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity

open access: yesNature Communications, 2018
A growing number of cargo-specific effector proteins are being identified that interact with both dynein and dynactin and form processive dynein-dynactin-effector complexes.
In-Gyun Lee   +5 more
doaj   +2 more sources

Cargo-Mediated Activation of Cytoplasmic Dynein in vivo

open access: yesFrontiers in Cell and Developmental Biology, 2020
Cytoplasmic dynein-1 is a minus-end-directed microtubule motor that transports a variety of cargoes including early endosomes, late endosomes and other organelles.
Xin Xiang, Rongde Qiu
doaj   +1 more source

Lissencephaly-1 is a context-dependent regulator of the human dynein complex

open access: yeseLife, 2017
The cytoplasmic dynein-1 (dynein) motor plays a central role in microtubule organisation and cargo transport. These functions are spatially regulated by association of dynein and its accessory complex dynactin with dynamic microtubule plus ends. Here, we
Janina Baumbach   +6 more
doaj   +1 more source

Kazrin promotes dynein/dynactin-dependent traffic from early to recycling endosomes

open access: yeseLife, 2023
Kazrin is a protein widely expressed in vertebrates whose depletion causes a myriad of developmental defects, in part derived from altered cell adhesion and migration, as well as failure to undergo epidermal to mesenchymal transition.
Ines Hernandez-Perez   +7 more
doaj   +1 more source

Nde1 promotes Lis1-mediated activation of dynein

open access: yesNature Communications, 2023
Cytoplasmic dynein drives the motility and force generation functions towards the microtubule minus end. The assembly of dynein with dynactin and a cargo adaptor in an active transport complex is facilitated by Lis1 and Nde1/Ndel1.
Yuanchang Zhao, Sena Oten, Ahmet Yildiz
doaj   +1 more source

Cortical dynein pulling mechanism is regulated by differentially targeted attachment molecule Num1

open access: yeseLife, 2018
Cortical dynein generates pulling forces via microtubule (MT) end capture-shrinkage and lateral MT sliding mechanisms. In Saccharomyces cerevisiae, the dynein attachment molecule Num1 interacts with endoplasmic reticulum (ER) and mitochondria to ...
Safia Omer   +2 more
doaj   +1 more source

From energy provision to protein synthesis: Tunnelling nanotubes as mediators of intercellular metabolic cooperation in cancer

open access: yesFEBS Open Bio, EarlyView.
The cytoskeleton‐mediated transport of mitochondria via tunnelling nanotubes restores respiration, increases ATP production, rescues cells from apoptosis, activates the AKT/mTOR signalling pathway, promotes cell migration and invasiveness, contributes to cancer progression and treatment resistance.
Stanislava Martínková, Jan Trnka
wiley   +1 more source

NuMA recruits dynein activity to microtubule minus-ends at mitosis

open access: yeseLife, 2017
To build the spindle at mitosis, motors exert spatially regulated forces on microtubules. We know that dynein pulls on mammalian spindle microtubule minus-ends, and this localized activity at ends is predicted to allow dynein to cluster microtubules into
Christina L Hueschen   +3 more
doaj   +1 more source

Home - About - Disclaimer - Privacy