Results 1 to 10 of about 6,766 (259)

Karyopherins regulate nuclear pore complex barrier and transport function [PDF]

Journal of Cell Biology, 2017
Nucleocytoplasmic transport is sustained by karyopherins (Kaps) and a Ran guanosine triphosphate (RanGTP) gradient that imports nuclear localization signal (NLS)–specific cargoes (NLS-cargoes) into the nucleus.
Larisa E. Kapinos, Binlu Huang, Chantal Rencurel, Roderick Y. H. Lim   +3 more
core   +10 more sources

Take your mother’s ferry: preimplantation embryo development requires maternal karyopherins for nuclear transport [PDF]

The Journal of Clinical Investigation, 2023
The genetic basis of preimplantation embryo arrest is slowly being unraveled. Recent discoveries point to maternally expressed proteins required for cellular functions before the embryonic genome is activated. In this issue of the JCI, Wang, Miyamoto, et
Momal Sharif, Laura Detti, Ignatia B. Van den Veyver   +2 more
doaj   +3 more sources

Nuclear transport proteins: structure, function and disease relevance [PDF]

Signal Transduction and Targeted Therapy, 2023
Proper subcellular localization is crucial for the functioning of biomacromolecules, including proteins and RNAs. Nuclear transport is a fundamental cellular process that regulates the localization of many macromolecules within the nuclear or cytoplasmic
Yang Yang, Lu Guo, Lin Chen, Bo Gong, Da Jia, Qingxiang Sun   +5 more
doaj   +2 more sources

Ibetazol, a novel inhibitor of importin β1-mediated nuclear import [PDF]

Communications Biology
Nucleocytoplasmatic transport plays an essential role in eukaryotic cell homeostasis and is mediated by karyopherins. Importin β1 (KPNB1) and its adaptor protein importin α1 (KPNA2) are the best-characterized karyopherins that effect nuclear import. Here,
Thomas Vercruysse, Els Vanstreels, Maarten Jacquemyn, Sandro Boland, Amuri Kilonda, Sara Allasia, Ilse Vandecaetsbeek, Hugo Klaassen, Matthias Versele, Patrick Chaltin, Arnaud Marchand, Dirk Daelemans   +11 more
doaj   +2 more sources

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

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   +3 more sources

Nuclear–Cytoplasmic Shuttling of the Usher Syndrome 1G Protein SANS Differs from Its Paralog ANKS4B [PDF]

Cells
The USH1G protein SANS is a small multifunctional scaffold protein. It is involved in several different cellular processes, such as intracellular transport, in the cytoplasm, or splicing of pre-mRNA, in the cell nucleus.
Jacques S. Fritze, Felizitas F. Stiehler, Uwe Wolfrum   +2 more
doaj   +2 more sources

Ran modulates allosteric crosstalk between importin β surfaces [PDF]

Nature Communications
A cellular gradient of the GTPase Ran orchestrates the movement of import and export complexes through the Nuclear Pore Complex (NPC). Ran-GTP modulates two essential activities of importin β during nuclear import. On the one hand, it reduces the avidity
Ying-Hui Ko, Fenglin Li, Stephanie S. Suinn, Junwei Li, Chun-Feng David Hou, Ravi K. Lokareddy, Gino Cingolani   +6 more
doaj   +2 more sources

Accumulation of TDP-43 causes karyopherin-α4 pathology that characterises amyotrophic lateral sclerosis [PDF]

Frontiers in Neuroscience
Cytoplasmic mislocalisation and nuclear depletion of TDP-43 are pathological hallmarks of amyotrophic lateral sclerosis (ALS), including mutations in the C9ORF72 gene that characterise the most common genetic form of ALS (C9ALS).
Manpreet Singh Atwal, Jerneja Nimac, Jerneja Nimac, Urša Čerček, Urša Čerček, Sarah Ricarda Goesch, Hannah Rebecca Goesch, Paraskevi Tziortzouda, Tiziana Ercolani, Anna Zatorska, Terouz Pasha, Ivo Carre, Jacqueline Mitchell, Claire Troakes, Bart Tummers, Vera Župunski, Boris Rogelj, Boris Rogelj, Tibor Hortobágyi, Tibor Hortobágyi, Frank Hirth   +20 more
doaj   +2 more sources

Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1 [PDF]

Scientific Reports
In eukaryotes, the ubiquitin–proteasome system is an essential pathway for protein degradation and cellular homeostasis. 26S proteasomes concentrate in the nucleus of budding yeast Saccharomyces cerevisiae due to the essential import adaptor protein Sts1
Carolyn Allain Breckel, Zane M. Johnson, Christopher M. Hickey, Mark Hochstrasser   +3 more
doaj   +2 more sources

HOX Protein Activity Regulation by Cellular Localization

Journal of Developmental Biology, 2021
While the functions of HOX genes have been and remain extensively studied in distinct model organisms from flies to mice, the molecular biology of HOX proteins remains poorly documented.
Laure Bridoux, Françoise Gofflot, René Rezsohazy   +2 more
doaj   +1 more source