Results 51 to 60 of about 6,495 (196)

Microtubule assembly by the Apc protein is regulated by importin-β—RanGTP [PDF]

Journal of Cell Science, 2010
Mutations in the tumour suppressor Adenomatous polyposis coli (Apc) initiate most sporadic colorectal cancers. Apc is implicated in regulating microtubule (MT) dynamics in interphase and mitosis. However, little is known about the underlying mechanism or regulation of this Apc function.
Dikovskaya, Dina, Li, Zhuoyu, Newton, Ian P., Davidson, Iain, Hutchins, James R. A., Kalab, Petr, Clarke, Paul R., Naethke, Inke S.   +7 more
openaire   +3 more sources

The Inner Nuclear Membrane Protein Nemp1 Is a New Type of RanGTP-Binding Protein in Eukaryotes. [PDF]

PLoS ONE, 2015
The inner nuclear membrane (INM) protein Nemp1/TMEM194A has previously been suggested to be involved in eye development in Xenopus, and contains two evolutionarily conserved sequences in the transmembrane domains (TMs) and the C-terminal region, named ...
Takashi Shibano, Hiroshi Mamada, Fumihiko Hakuno, Shin-Ichiro Takahashi, Masanori Taira   +4 more
doaj   +1 more source

The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.

PLoS ONE, 2015
Molecular traffic between the nucleus and the cytoplasm is regulated by the nuclear pore complex (NPC), which acts as a highly selective channel perforating the nuclear envelope in eukaryotic cells.
Seyed Hanif Mahboobi, Alex A Javanpour, Mohammad R K Mofrad   +2 more
doaj   +1 more source

Identification of Two Novel RanGTP-binding Proteins Belonging to the Importin β Superfamily [PDF]

Journal of Biological Chemistry, 2000
Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin beta superfamily of nuclear transport receptors. These transport receptors all directly interact with RanGTP to modulate the compartment-specific binding of their transport substrates.
Kutay, U., Hartmann, E., Treichel, N., Calado, A., Carmo-Fonseca, M., Prehn, S., Kraft, R., Görlich, D., Bischoff, F.   +8 more
openaire   +4 more sources

Karyopherin binding interactions and nuclear import mechanism of nuclear pore complex protein Tpr [PDF]

, 2009
Background Tpr is a large protein with an extended coiled-coil domain that is localized within the nuclear basket of the nuclear pore complex. Previous studies 1 involving antibody microinjection into mammalian cells suggested a role for Tpr in nuclear ...
Iris Ben-Efraim, Phyllis D Frosst, Larry Gerace   +2 more
core   +2 more sources

A thermodynamic paradigm for solution demixing inspired by nuclear transport in living cells

, 2017
Living cells display a remarkable capacity to compartmentalize their functional biochemistry. A particularly fascinating example is the cell nucleus. Exchange of macromolecules between the nucleus and the surrounding cytoplasm does not involve traversing
Elbaum, Michael, Mehta, Pankaj, Wang, Ching-Hao   +2 more
core   +1 more source

The Nuclear Transport Factor Kap121 Is Required for Stability of the Dam1 Complex and Mitotic Kinetochore Bi-orientation

Cell Reports, 2016
The karyopherin (Kap) family of nuclear transport factors facilitates macromolecular transport through nuclear pore complexes (NPCs). The binding of Kaps to their cargos can also regulate, both temporally and spatially, the interactions of the cargo ...
Lucas V. Cairo, Richard W. Wozniak
doaj   +1 more source

Disassembly of RanGTP-Karyopherin β Complex, an Intermediate in Nuclear Protein Import [PDF]

Journal of Biological Chemistry, 1997
We previously showed that RanGTP forms a 1:1 complex with karyopherin beta that renders RanGTP inaccessible to RanGAP (Floer, M., and Blobel, G. (1996) J. Biol. Chem. 271, 5313-5316) and karyopherin beta functionally inactive (Rexach, M., and Blobel, G. (1995) Cell 83, 683-692).
M, Floer, G, Blobel, M, Rexach
openaire   +2 more sources

eEF1A mediates the nuclear export of SNAG-containing proteins via the exportin5-aminoacyl-tRNA complex [PDF]

, 2015
This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License.Exportin5 mediates the nuclear export of double-stranded RNAs, including pre-microRNAs, adenoviral RNAs, and tRNAs ...
Cano, Amparo, Mingot, José Manuel, Nieto, M. Ángela, Portillo, Francisco, Vega, Sonia   +4 more
core   +1 more source

DnaJB6 is a RanGTP-regulated protein required for microtubule organization during mitosis [PDF]

Journal of Cell Science, 2019
ABSTRACT Bipolar spindle organization is essential for the faithful segregation of chromosomes during cell division. This organization relies on the collective activities of motor proteins. The minus-end-directed dynein motor complex generates spindle inward forces and plays a major role in spindle pole focusing.
Miquel Rosas-Salvans, Jacopo Scrofani, Aitor Modol, Isabelle Vernos   +3 more
openaire   +3 more sources