Results 11 to 20 of about 6,766 (259)
Current Opinion in Cell Biology, 2020 Several aggregation-prone RNA-binding proteins, including FUS, EWS, TAF15, hnRNP A1, hnRNP A2, and TDP-43, are mutated in neurodegenerative diseases. The nuclear-cytoplasmic distribution of these proteins is controlled by proteins in the karyopherin family of nuclear transport factors (Kaps). Recent studies have shown that Kaps not only transport these
Charis E Springhower, M. Rosen, Y. Chook
semanticscholar +3 more sources
Current Opinion in Cell Biology, 2018 Malfunction of nuclear-cytoplasmic transport contributes to many diseases including cancer. Defective nuclear transport leads to changes in both the physiological levels and temporal-spatial location of tumor suppressors, proto-oncogenes and other macromolecules that in turn affect the tumorigenesis process and drug sensitivity of cancer cells.
T. Cagatay, Y. Chook
semanticscholar +4 more sources
Birth, Death, and Replacement of Karyopherins in Drosophila [PDF]
Molecular Biology and Evolution, 2011 Nucleocytoplasmic transport is a broadly conserved process across eukaryotes. Despite its essential function and conserved mechanism, components of the nuclear transport apparatus have been implicated in genetic conflicts in Drosophila, especially in the male germ line. The best understood case is represented by a truncated RanGAP gene duplication that
Nitin Phadnis +2 more
semanticscholar +4 more sources
Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2014 Nucleocytoplasmic transport is facilitated by nuclear pore complexes (NPCs), which are massive proteinaceous transport channels embedded in the nuclear envelope.
Collins, Leslie N. +4 more
core +2 more sources
Karyopherins in nuclear pore biogenesis [PDF]
The Journal of Cell Biology, 2002 The mechanisms that govern the assembly of nuclear pore complexes (NPCs) remain largely unknown. Here, we have established a role for karyopherins in this process.
C. Lusk +4 more
semanticscholar +2 more sources
Importins/Karyopherins Meet Nucleoporins [PDF]
Cell, 1996 I thank Gunter Blobel, Valerie Doye, Dirk Gorlich, Iain Mattaj, Ulf Nehrbass, and Uli Scheer for helpful comments on the manuscript.
E. Hurt
semanticscholar +2 more sources
Karyopherins play the field [PDF]
The Journal of Cell Biology, 2006 ![][1] Import of proteins (green) into the nucleus is slower than expected, revealing that karyopherins are choosy about their cargo. Proteins that shuttle molecules into the nucleus face the same problem as customers of a dating service.
M. Leslie
semanticscholar +2 more sources
Adjunct duties for karyopherins: regulating septin sumoylation. [PDF]
Developmental Cell, 2007 Karyopherins are shuttling transport receptors regulated by the small GTPase Ran, which move cargo between the nucleus and cytoplasm by passing through the nuclear pore complexes. A recent paper in Journal of Cell Biology (Makhnevych et al., 2007) highlights an additional role for karyopherins during mitosis, in regulating the sumoylation status of the
V. G. Panse, E. Hurt
semanticscholar +3 more sources
Karyopherins in nuclear transport of homeodomain proteins during development.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2011 Homeodomain proteins are crucial transcription factors for cell differentiation, cell proliferation and organ development. Interestingly, their homeodomain signature structure is important for both their DNA-binding and their nucleocytoplasmic trafficking.
Wenduo Ye +3 more
semanticscholar +4 more sources
The HIV capsid mimics karyopherin engagement of FG-nucleoporins. [PDF]
NatureHIV can infect non-dividing cells because the viral capsid can overcome the selective barrier of the nuclear pore complex and deliver the genome directly into the nucleus1,2. Remarkably, the intact HIV capsid is more than 1,000 times larger than the size
Dickson CF +12 more
europepmc +5 more sources