منابع مشابه
Localization of the gene encoding the Ran-binding protein RanBP2 to human chromosome 2q11-q13 by fluorescence in situ hybridization.
liams, S., McDermid, H., Dumanski, J. P., Biegel, J., Bell, C. J., 14. Takeuchi, K., Takahashi, K., Abe, M., Nishida, W., Hiwada, K., Nabeya, T., and Maruyama, K. (1991). Co-localization of and Emanuel, B. S. (1996). Regional localization of over 300 loci on human chromosome 22 using a somatic cell hybrid mapping immunoreactive forms of calponin with actin cytoskeleton in platelets, fibroblasts...
متن کاملSmall GTPase Ran and Ran-binding proteins.
Abstract Like many other small GTPases, Ran functions in eukaryotic cells as a molecular switch that cycles between GTP- and GDP-bound forms. Through the proper modulation of the GTP/GDP cycle, Ran functions with a number of Ran-binding proteins to control a broad array of fundamental cellular functions, including nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope and n...
متن کاملThe Ran-binding protein-2 (RanBP2) is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system
The Ran-binding protein-2 (RanBP2) is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. Kyoung-in Cho, Haiqing Yi, Ria Desai, Arthur R. Hand, Arthur L. Haas and Paulo A. Ferreira* 1, 4 Department of Ophthalmology, Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710 Departments of Craniofacia...
متن کاملFacilitated nucleocytoplasmic shuttling of the Ran binding protein RanBP1.
The Ran binding protein RanBP1 is localized to the cytosol of interphase cells. A leucine-rich nuclear export signal (NES) near the C terminus of RanBP1 is essential to maintain this distribution. We now show that RanBP1 accumulates in nuclei of cells treated with the export inhibitor, leptomycin B, and collapse of the nucleocytoplasmic Ran:GTP gradient leads to equilibration of RanBP1 across t...
متن کاملRan-dependent docking of importin-β to RanBP2/Nup358 filaments is essential for protein import and cell viability
RanBP2/Nup358, the major component of the cytoplasmic filaments of the nuclear pore complex (NPC), is essential for mouse embryogenesis and is implicated in both macromolecular transport and mitosis, but its specific molecular functions are unknown. Using RanBP2 conditional knockout mouse embryonic fibroblasts and a series of mutant constructs, we show that transport, rather than mitotic, funct...
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ژورنال
عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology
سال: 2011
ISSN: 1768-3262
DOI: 10.4267/2042/38011