The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex

Article Abstract:

Nup98, a nuclear pore complex (NPC) protein of rat, has been identified as a new mammalian member of the nucleoporin family, one which has many GLFG and FG repeat sequences. It is located in the nucleoplasmic site of the NPC, and the N-terminal repeat sequences have been reported to be involved in the cytosol-dependent binding of the ligand. The repeat sequences thus act as docking sites, where transport across NPC takes place by docking and un-docking reactions at these sites. Molecular characterization of this protein has also been reported.

Amino acid sequence, Amino acid sequencing

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A distinct nuclear import pathway used by ribosomal proteins

Article Abstract:

The role of the Kap123p yeast beta karyopherin in the transport of ribosomal proteins in the nucleolus was analyzed to characterize the mechanisms that mediate different nuclear import pathways. Analysis of the protein kinetics of the yeast beta karyopherin in a highly enriched nuclear pore complex fraction from yeasts indicated the ability of Kap123p to bind directly with its transport substrates. Furthermore, the beta karyopherin specifically recognized 15 and 50 kilodalton ribonucleoproteins.

Biological transport, Active, Active biological transport

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Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins

Article Abstract:

Protein import into nucleus involves the association of the karyopherin alpha/beta transport factors with the FXFG repeats of nucleoporins, and dissociation of the heterodimer. In the presence of a FXFG region, the protein nuclear localization signal and karyopherin alpha/beta heterodimer complex dissociates. The karyopherin beta part of the heterodimer then binds to the FXFG region. RanGTP causes the dissociation and release of the heterodimer from FXFG.

Observations, Proteins, Cell nuclei, Cell nucleus

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