Results 161 to 170 of about 3,763 (189)
Small molecule JRMS modulating importin-β1 chaperone activity as a therapeutic strategy reducing TDP-43 pathology. [PDF]
Shenouda M +5 more
europepmc +1 more source
LINC1467 Activates the IPO8-p65 Axis to Restrict Hand, Foot, and Mouth Disease Virus Replication. [PDF]
Zhang X +6 more
europepmc +1 more source
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.
Tolga Cagatay, Yuh Min Chook
exaly +5 more sources
Karyopherins in nuclear pore biogenesis [PDF]
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. We show that the yeast karyopherin Kap121p functions in the targeting and assembly of the nucleoporin Nup53p into NPCs by recognizing a nuclear localization signal (NLS) in Nup53p.
C Patrick Lusk +2 more
exaly +3 more sources
The role of karyopherins in the regulated sumoylation of septins [PDF]
In the yeast Saccharomyces cerevisiae, several components of the septin ring are sumoylated during anaphase and then abruptly desumoylated at cytokinesis. We show that septin sumoylation is controlled by the interactions of two enzymes of the sumoylation pathway, Siz1p and Ulp1p, with the nuclear transport machinery.
C Patrick Lusk +2 more
exaly +4 more sources
Karyopherins in nuclear transport of homeodomain proteins during development
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, Wenbo Lin, Alan M Tartakoff
exaly +5 more sources
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
Michael K Rosen, Yuh Min Chook
exaly +3 more sources
Karyopherins regulate nuclear pore complex barrier and transport function [PDF]
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 +2 more
exaly +2 more sources
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Karyopherin-mediated nucleocytoplasmic transport
Nature Reviews Molecular Cell Biology, 2022Efficient and regulated nucleocytoplasmic trafficking of macromolecules to the correct subcellular compartment is critical for proper functions of the eukaryotic cell. The majority of the macromolecular traffic across the nuclear pores is mediated by the Karyopherin-β (or Kap) family of nuclear transport receptors.
Casey E. Wing +2 more
openaire +2 more sources

