WDR60-mediated dynein-2 loading into cilia powers retrograde IFT and transition zone crossing [PDF]
, 2022 The dynein-2 motor complex drives retrograde intraflagellar transport (IFT), playing a pivotal role in the assembly and functions of cilia. However, the mechanisms that regulate dynein-2 motility remain poorly understood.
Dantas, T +8 more
core +1 more source
Nde1 promotes Lis1-mediated activation of dynein
Nature 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
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 +1 more source
A single protofilament is sufficient to support unidirectional walking of dynein and kinesin. [PDF]
PLoS ONE, 2012 Cytoplasmic dynein and kinesin are two-headed microtubule motor proteins that move in opposite directions on microtubules. It is known that kinesin steps by a 'hand-over-hand' mechanism, but it is unclear by which mechanism dynein steps.
Keitaro Shibata +6 more
doaj +1 more source
Dynein modifiers in C. elegans: light chains suppress conditional heavy chain mutants. [PDF]
PLoS Genetics, 2007 Cytoplasmic dynein is a microtubule-dependent motor protein that functions in mitotic cells during centrosome separation, metaphase chromosome congression, anaphase spindle elongation, and chromosome segregation. Dynein is also utilized during interphase
Sean M O'Rourke +3 more
doaj +1 more source
Structure of a microtubule-bound axonemal dynein
Nature Communications, 2021 Axonemal dyneins are tethered to doublet microtubules inside cilia to drive ciliary beating, a process critical for cellular motility and extracellular fluid flow.
T. Walton, Hao Wu, Alan Brown
semanticscholar +1 more source
Lis1 activates dynein motility by modulating its pairing with dynactin
Nature Cell Biology, 2020 Lissencephaly-1 (Lis1) is a key cofactor for dynein-mediated intracellular transport towards the minus-ends of microtubules. It remains unclear whether Lis1 serves as an inhibitor or an activator of mammalian dynein motility.
M. M. ElShenawy +5 more
semanticscholar +1 more source
Structural basis for cytoplasmic dynein-1 regulation by Lis1
bioRxiv, 2021 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 ...
J. P. Gillies +6 more
semanticscholar +1 more source
Mitotic control of kinetochore-associated dynein and spindle orientation by human Spindly [PDF]
, 2009 Mitotic spindle formation and chromosome segregation depend critically on kinetochore-microtubule (KT-MT) interactions. A new protein, termed Spindly in Drosophila and SPDL-1 in C.
Erich A. Nigg +15 more
core +1 more source
Sequential dynein effectors regulate axonal autophagosome motility in a maturation-dependent pathway
bioRxiv, 2020 Autophagy is a degradative pathway required to maintain neuronal homeostasis. Neuronal autophagosomes form constitutively at the axon terminal and mature via lysosomal fusion during dynein-mediated transport to the soma.
Sydney E. Cason +5 more
semanticscholar +1 more source