نتایج جستجو برای: ran

تعداد نتایج: 9987  

Journal: :Journal of cell science 1999
W Feng A L Benko J H Lee D R Stanford A K Hopper

Nucleus/cytosol exchange requires a GTPase, Ran. In yeast Rna1p is the GTPase activating protein for Ran (RanGAP) and Prp20p is the Ran GDP/GTP exchange factor (GEF). RanGAP is primarily cytosolic and GEF is nuclear. Their subcellular distributions led to the prediction that Ran-GTP hydrolysis takes place solely in the cytosol and GDP/GTP exchange solely in the nucleus. Current models propose t...

Journal: :Molecular biology of the cell 2004
Ian Cushman David Stenoien Mary Shannon Moore

Regulator of chromosome condensation (RCC1) binding to chromatin is highly dynamic, as determined by fluorescence recovery after photobleaching analysis of GFP-RCC1 in stably transfected tsBN2 cells. Microinjection of wild-type or Q69L Ran markedly slowed the mobility of GFP-RCC1, whereas T24N Ran (defective in nucleotide loading) decreased it further still. We found significant alterations in ...

2014
Yong Wook Jung Young Joo Jeon HyungChul Rah Ji Hyang Kim Ji Eun Shin Dong Hee Choi Sun Hee Cha Nam Keun Kim

OBJECTIVE Key molecules involved in microRNA (miRNA) biogenesis, such as DROSHA, XPO5, and DICER, have been identified in trophoblast cells, confirming that the miRNA biogenesis pathway is active in human placenta. In addition, miRNAs regulate uterine gene expression associated with inflammatory responses during the peri-implantation period and participate in maternal-fetal immune tolerance. Th...

Journal: :Journal of cell science 1997
F J Nicolás C Zhang M Hughes M W Goldberg S J Watton P R Clarke

Ran is a nuclear GTPase implicated in nucleocytoplasmic transport, the maintenance of nuclear structure, mRNA processing, and cell cycle regulation. By two-hybrid interaction in yeast, we have identified a Xenopus homologue of Ran-binding protein 1 (RanBP1). Xenopus RanBP1 interacts specifically with the GTP-bound form of Ran and forms complexes in Xenopus egg extracts with Ran, importin-beta/k...

2016
Pavol Cekan Keisuke Hasegawa Yu Pan Emily Tubman David Odde Jin-Qiu Chen Michelle A. Herrmann Sheetal Kumar Petr Kalab

The coordination of cell cycle progression with the repair of DNA damage supports the genomic integrity of dividing cells. The function of many factors involved in DNA damage response (DDR) and the cell cycle depends on their Ran GTPase-regulated nuclear-cytoplasmic transport (NCT). The loading of Ran with GTP, which is mediated by RCC1, the guanine nucleotide exchange factor for Ran, is critic...

Journal: :Cell 1996
Deanna M Koepp Pamela A Silver

In addition, certain GTP analogs inhibit nuclear import, indicating that GTP hydrolysis by Ran is neces-Macromolecular movement across the nuclear envelope sary for proper nuclear protein import. Failure by Ran is distinctly bidirectional. Proteins are targeted to and to hydrolyze and/or exchange nucleotide also results in enter the nucleus at nuclear pore complexes (NPCs) in a block in RNA exp...

Journal: :Computer Networks 2017
Sangkyu Park Hyunjoong Lee Chan-Byoung Chae Saewoong Bahk

Massive multiple-input multiple-output (MIMO) is considered as one of the key technologies in next generation cellular systems due to its higher multiplexing gain and energy efficiency. However, in a cloud radio access network (C-RAN) with massive MIMO, operation of many antennas incurs a huge amount of digital sampled data to be transported over the fronthaul link between a baseband unit (BBU)...

Journal: :Journal of molecular biology 2009
James R Partridge Thomas U Schwartz

The nuclear pore complex (NPC) resides in circular openings within the nuclear envelope and serves as the sole conduit to facilitate nucleocytoplasmic transport in eukaryotes. The asymmetric distribution of the small G protein Ran across the nuclear envelope regulates directionality of protein transport. Ran interacts with the NPC of metazoa via two asymmetrically localized components, Nup153 a...

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