Results 1 to 10 of about 3,517 (188)

Motorless transport of microtubules along tubulin, RanGTP, and salt gradients [PDF]

Nature Communications
Microtubules are dynamic filaments that assemble spindles for eukaryotic cell division. As the concentration profiles of soluble tubulin and regulatory proteins are non-uniform during spindle assembly, we asked if diffusiophoresis - motion of particles ...
Suin Shim, Bernardo Gouveia, Beatrice Ramm, Venecia A. Valdez, Sabine Petry, Howard A. Stone   +5 more
doaj   +7 more sources

XPO5 promotes primary miRNA processing independently of RanGTP [PDF]

Nature Communications, 2020
XPO5 mediates nuclear export of miRNA hairpin precursors (pre-miRNAs) through a RanGTP-dependent binding. Here the authors employ HITS-CLIP and biochemical analysis and show that XPO5 binds and promotes nuclear processing of clustered pri-miRNAs, with ...
Jingjing Wang, Jerome E. Lee, Kent Riemondy, Yang Yu, Steven M. Marquez, Eric C. Lai, Rui Yi   +6 more
doaj   +3 more sources

A multivalent adaptor mechanism drives the nuclear import of proteasomes [PDF]

Nature Communications
Nuclear protein homeostasis, including transcription factor turnover, critically depends on the nuclear proteasomes that must be imported after cell division.
Hanna L. Brunner, Robert W. Kalis, Lorenz Grundmann, Zuzana Hodáková, Zuzana Koskova, Irina Grishkovskaya, Melanie de Almeida, Matthias Hinterndorfer, Hannah Knaudt, Simon Höfflin, Florian Andersch, Harald Kotisch, Achim Dickmanns, Sara Cuylen-Haering, Johannes Zuber, David Haselbach   +15 more
doaj   +2 more sources

γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end

EMBO Journal
The γ-tubulin ring complex (γ-TuRC) is a structural template for de novo microtubule assembly from α/β-tubulin units. The isolated vertebrate γ-TuRC assumes an asymmetric, open structure deviating from microtubule geometry, suggesting that γ-TuRC closure
Stefan Pfeffer, Oliver J Gruss, Elmar Schiebel   +2 more
exaly   +2 more sources

HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2 [PDF]

Nature Communications
In vertebrate spindles, most microtubules are formed via branching microtubule nucleation, whereby microtubules nucleate along the side of pre-existing microtubules.
Venecia Alexandria Valdez, Meisheng Ma, Bernardo Gouveia, Rui Zhang, Sabine Petry   +4 more
doaj   +2 more sources

Self-organization of anastral spindles by synergy of dynamic instability, autocatalytic microtubule production, and a spatial signaling gradient. [PDF]

PLoS ONE, 2007
Assembly of the mitotic spindle is a classic example of macromolecular self-organization. During spindle assembly, microtubules (MTs) accumulate around chromatin.
Thomas Clausen, Katharina Ribbeck
doaj   +1 more source

Distinct RanBP1 nuclear export and cargo dissociation mechanisms between fungi and animals

eLife, 2019
Ran binding protein 1 (RanBP1) is a cytoplasmic-enriched and nuclear-cytoplasmic shuttling protein, playing important roles in nuclear transport. Much of what we know about RanBP1 is learned from fungi. Intrigued by the long-standing paradox of harboring
Yuling Li, Jinhan Zhou, Sui Min, Yang Zhang, Yuqing Zhang, Qiao Zhou, Xiaofei Shen, Da Jia, Junhong Han, Qingxiang Sun   +9 more
doaj   +1 more source

Meiotic regulation of TPX2 protein levels governs cell cycle progression in mouse oocytes. [PDF]

PLoS ONE, 2008
Formation of female gametes requires acentriolar spindle assembly during meiosis. Mitotic spindles organize from centrosomes and via local activation of the RanGTPase on chromosomes.
Stéphane Brunet, Julien Dumont, Karen W Lee, Kazuhisa Kinoshita, Pascale Hikal, Oliver J Gruss, Bernard Maro, Marie-Hélène Verlhac   +7 more
doaj   +1 more source

Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner

eLife, 2015
Soluble karyopherins of the importin-β (impβ) family use RanGTP to transport cargos directionally through the nuclear pore complex (NPC). Whether impβ or RanGTP regulate the permeability of the NPC itself has been unknown.
Alan R Lowe, Jeffrey H Tang, Jaime Yassif, Michael Graf, William YC Huang, Jay T Groves, Karsten Weis, Jan T Liphardt   +7 more
doaj   +1 more source

Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A

eLife, 2020
In the nucleus, the spatiotemporal regulation of the catalytic subunit of cAMP-dependent protein kinase A (PKA-C) is orchestrated by an intrinsically disordered protein kinase inhibitor, PKI, which recruits the CRM1/RanGTP nuclear exporting complex.
Cristina Olivieri, Yingjie Wang, Geoffrey C Li, Manu V S, Jonggul Kim, Benjamin R Stultz, Matthew Neibergall, Fernando Porcelli, Joseph M Muretta, David DT Thomas, Jiali Gao, Donald K Blumenthal, Susan S Taylor, Gianluigi Veglia   +13 more
doaj   +1 more source