Results 21 to 30 of about 14,978 (204)

Microtubules gate tau condensation to spatially regulate microtubule functions. [PDF]

, 2019
Tau is an abundant microtubule-associated protein in neurons. Tau aggregation into insoluble fibrils is a hallmark of Alzheimer's disease and other types of dementia1, yet the physiological state of tau molecules within cells remains unclear.
A Ettinger, A Hernandez-Vega, A Kremer, A Seitz, Aileen J. Lam, AR Duan, B Niewidok, BY Monroy, Dan W. Nowakowski, DP McVicker, DP McVicker, EH Kellogg, H Hagiwara, H Zempel, HT Hoang, J Baumbach, JA Garcia-Leon, Jisoo Han, K Tepper, Kassandra M. Ori-McKenney, KM Ori-McKenney, KS Hubbard, L Qiang, L Urnavicius, LC Kapitein, M Goedert, M Vershinin, M Vershinin, MH Hinrichs, Michael Vershinin, PA Gutierrez, R Dixit, R Zhang, RD Vale, Richard J. McKenney, RJ McKenney, RJ McKenney, Ruensern Tan, S Ambadipudi, S Konzack, S Wegmann, S Wegmann, Sergi Simó, SR White, Tracy Tan, V Makrides, W Yu, XH Li   +47 more
core   +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.
Deacon, Sean W., Serpinskaya, Anna S., Vaughan, Patricia S., Fanarraga, Monica Lopez, Vernos, Isabelle, Vaughan, Kevin T., Gelfand, Vladimir I.   +6 more
openaire   +2 more sources

The actin capping protein in Aspergillus nidulans enhances dynein function without significantly affecting Arp1 filament assembly

Scientific 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

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus [PDF]

, 2004
The tumor suppressor protein p53 is known to be transported to the nucleus along microtubular tracks by cytoplasmic dynein. However, the connection between p53 and the dynein motor protein complex has not been established.
Galigniana, Mario Daniel, Harrell, Jennifer M., Ljungman, Mats, O´Hagen, Heather M., Pratt, William B.   +4 more
core   +1 more source

Dynein Regulators Are Important for Ecotropic Murine Leukemia Virus Infection [PDF]

, 2016
Indexación: Web of Science.During the early steps of infection, retroviruses must direct the movement of the viral genome into the nucleus to complete their replication cycle.
Arriagada, Gloria, Cancino, Jorge, Goff, Stephen P., Opazo, Tatiana, Valle-Tenney, Roger   +4 more
core   +1 more source

CENP-F stabilizes kinetochore-microtubule attachments and limits dynein stripping of corona cargoes [PDF]

, 2020
Accurate chromosome segregation demands efficient capture of microtubules by kinetochores and their conversion to stable bioriented attachments that can congress and then segregate chromosomes.
Allan, Andrew D. McAinsh, Auckland, Bancroft, Baumbach, Berto, Berto, Bolhy, Bomont, Chan, Ciossani, Currie, DeSantis, Dix, Dudka, Emanuele Roscioli, Etemad, Faulkner, Feng, Filges, Gama, Gassmann, Gutierrez, Haley, Helena Louise Elvidge Coker, Helgeson, Hoffman, Holt, Howell, Huang, Huis In ’t Veld, Johnson, Kanfer, Kanfer, Klinman, Kuhn, Liu, Magidson, Magidson, Maiato, McEwen, McEwen, McKinley, Meraldi, Monda, Moughamian, Musacchio, Musacchio, Musinipally, Olenick, Olziersky, Pandey, Pereira, Peterka, Philip Auckland, Raaijmakers, Ran, Rattner, Rodriguez-Rodriguez, Roscioli, Sacristan, Samejima, Schmidt, Shao, Shrestha, Siller, Simões, Stehman, Tai, Thrower, Toropova, Vagnoni, Vergnolle, Volkov, Wojcik, Wynne, Wynne, Wynne, Yang, Yi, Zhu   +80 more
core   +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 ...
Karin A, Melkonian, Kerstin C, Maier, Jamie E, Godfrey, Michael, Rodgers, Trina A, Schroer   +4 more
openaire   +2 more sources

New insights into the mechanism of dynein motor regulation by lissencephaly-1

eLife, 2020
Lissencephaly (‘smooth brain’) is a severe brain disease associated with numerous symptoms, including cognitive impairment, and shortened lifespan. The main causative gene of this disease – lissencephaly-1 (LIS1) – has been a focus of intense scrutiny ...
Steven M Markus, Matthew G Marzo, Richard J McKenney   +2 more
doaj   +1 more source

Cyclophilin-A is bound to through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex [PDF]

, 2004
Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known.
Galigniana, Mario Daniel, Gallay, Philippe A., Morishima, Yoshihiro, Pratt, William B.   +3 more
core   +2 more sources

Dynactin polices two-way organelle traffic [PDF]

The Journal of Cell Biology, 2003
How is the bidirectional motion of organelles controlled? In this issue, Deacon et al. (2003) reveal the unexpected finding that dynactin (previously known to control dynein-based motility) binds to kinesin II and regulates anterograde movement of Xenopus melanosomes.
openaire   +2 more sources