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

By A. Radu, M. Moore, Günter Blobel. 1995

We report the cDNA deduced primary structure of a wheat germ agglutinin-reactive nuclear pore complex (NPC) protein of rat. The protein, termed Nup98 (for nucleoporin of 98 kDa), contains numerous GLFG and FG repeats and some FXFG repeats and is thus a vertebrate member of a family of GLFG nucleoporins that were previously discovered in yeast. Immunoelectron microscopy showed Nup98 to be asymmetrically located at the nucleoplasmic side of the NPC. Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate. The docking site of Nup98 was mapped to its N-terminal half, which contains all of the peptide repeats. A recombinant segment of this region depleted the docking activity of cytosol. We suggest that the peptide repeat domain of Nup98, together with peptide repeat domains of other nucleoporins, forms an array of sites for mediated docking of transport substrate, and that bidirectional transport across the NPC proceeds by repeated docking and undocking reactions.

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Citations in the corpus

SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling (2020, methodology): “After 24 h, cell lysates were subjected to immunoprecipitations with an anti-Nup98 antibody (45).”
The nuclear pore complex: bridging nuclear transport and gene regulation (2010, background): “21 ) make up as much as one-third of the molecular mass of the NPC and have a pivotal role in determining the mechanism of nuclear transport as they contain the docking sites for most NTF–cargo complexes en route through the NP”
The nuclear pore complex and nuclear transport. (2010, background): “Both processes are dependent on the correct positioning of critical Nups in the NPC architecture (Radu et al. 1995; Strawn et al. 2004; Liu and Stewart 2005).”
Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1•Nup98) (2014, methodology): “The model of M•Rae1•Nup98 was built using Coot (5) and refined using Refmac (6).”
Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, unknown): “The FG repeats interact with nuclear transport receptors, providing a selective barrier to the diffusion of macromolecules (Radu et al., 1995; Patel et al., 2007).”
The Yeast Nuclear Pore Complex (2000, unknown): “…NPCs for various transport factors are composed of a specific subset of nups that contains degenerate Phe-Gly repeats (FG nups) and appear to constitute most of the filamentous structures emanating from the NPC (Buss et al., 1994; Radu et al., 1995; Katahira et al., 1999; Kehlenbach et al., 1999).”