Results 11 to 20 of about 17,522 (280)

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

eLife, 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, Javier Rubio, Adrian Baumann, Henrique Girao, Miriam Ferrando, Elena Rebollo, Anna M Aragay, María Isabel Geli   +7 more
doaj   +2 more sources

RUFY3 and RUFY4 are ARL8 effectors that promote coupling of endolysosomes to dynein-dynactin

Nature Communications, 2022
Organellar transport is carefully regulated, and endolysosome localized ARL8 is important for kinesin recruitment and anterograde movement. Here, the authors show that RUFY3 and RUFY4 promote retrograde transport of endolysosomes by mediating interaction
Tal Keren-Kaplan, Amra Sarić, Saikat Ghosh, Chad D. Williamson, Rui Jia, Yan Li, Juan S. Bonifacino   +6 more
doaj   +2 more sources

Dynein and dynactin move long-range but are delivered separately to the axon tip [PDF]

bioRxiv, 2023
Axonal transport is essential for neuronal survival. This is driven by microtubule motors including dynein, which transports cargo from the axon tip back to the cell body. This function requires its cofactor dynactin and regulators LIS1 and NDEL1. Due to
Alexander D. Fellows, Michaela Bruntraeger, Thomas Burgold, Andrew Bassett, Andrew P. Carter   +4 more
semanticscholar   +4 more sources

Cargo adaptors regulate stepping and force generation of mammalian dynein-dynactin. [PDF]

Nature Chemical Biology, 2019
Cytoplasmic dynein is an ATP-driven motor that transports intracellular cargos along microtubules. Dynein adopts an inactive conformation when not attached to a cargo, and motility is activated when dynein assembles with dynactin and a cargo adaptor.
Blanchard, Scott C, Canty, John T, Elshenawy, Mohamed M, Ferro, Luke S, Oster, Liya, Yildiz, Ahmet, Zhou, Zhou   +6 more
core   +2 more sources

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

Nature 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, Mara A. Olenick, Malgorzata Boczkowska, Clara Franzini-Armstrong, Erika L. F. Holzbaur, Roberto Dominguez   +5 more
doaj   +2 more sources

Dynein–Dynactin–NuMA clusters generate cortical spindle-pulling forces as a multi-arm ensemble

eLife, 2018
To position the mitotic spindle within the cell, dynamic plus ends of astral microtubules are pulled by membrane-associated cortical force-generating machinery.
Masako Okumura, Toyoaki Natsume, Masato T Kanemaki, Tomomi Kiyomitsu   +3 more
doaj   +2 more sources

Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin [PDF]

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 d’Amico, Misbha Ud Din Ahmad, Verena Cmentowski, Mathias Girbig, Franziska Müller, Sabine Wohlgemuth, Andreas Brockmeyer, Stefano Maffini, Petra Janning, Ingrid R. Vetter, Andrew P. Carter, Anastassis Perrakis, Arianna Esposito Verza   +12 more
openalex   +2 more sources

N4BP2L1 interacts with dynactin and contributes to GLUT4 trafficking and glucose uptake in adipocytes

Journal of Diabetes Investigation, 2021
Aims/Introduction It was reported previously that N4bp2l1 expression increases in 3T3‐L1 cells in a differentiation‐dependent manner and N4bp2l1 knockdown suppresses adipocyte differentiation.
Kazuhisa Watanabe, Ayumi Matsumoto, Hidetoshi Tsuda, Sadahiko Iwamoto   +3 more
doaj   +2 more sources

Multivalency, autoinhibition, and protein disorder in the regulation of interactions of dynein intermediate chain with dynactin and the nuclear distribution protein

bioRxiv, 2022
Cytoplasmic dynein plays crucial roles in the intracellular transport of organelles and other cargoes. Central to dynein function is the intrinsically disordered N-terminal domain of dynein intermediate chain (IC), which binds the three dimeric dynein ...
Kayla A. Jara, Nikolaus M. Loening, Patrick N. Reardon, Zhen Yu, Prajna Woonnimani, Coban Brooks, Cat Hoang Vesely, Elisar Barbar   +7 more
openalex   +2 more sources

CDKL5 regulates the initiation of retrograde axonal transport through CLIP170-dynactin complex formation. [PDF]

FEBS J
Activation of CLIP170 by CDKL5 in wild‐type (WT) cells promotes its open conformation and association with tyrosinated microtubule (MT) plus‐ends (+), where it works as a docking site to recruit the dynactin–dynein–cargo complex, promoting the initiation of retrograde transport. In knock‐out (KO) neurons, CLIP170 is mainly present in a closed (inactive)
Baldin S, Carmone C, Valetti G, De Rosa R, Barbiero I.   +4 more
europepmc   +2 more sources