Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1

By Yi Ren, H. Seo, Günter Blobel, A. Hoelz. 2010

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In Molecular Biology

Citations in the corpus

Sarbecovirus ORF6 proteins hamper induction of interferon signaling (2021, unknown): “Although RAE1 exports RNA from the nucleus, NUP98 is a component of the nuclear pore complex (Pritchard et al., 1999; Ren et al., 2010).”
Bub3 reads phosphorylated MELT repeats to promote spindle assembly checkpoint signaling (2013, background): “Most of the residues involved in MELTP binding on Bub3 are perfectly conserved in Rae1 (Figure 2C), where they form a hydrophobic-basic bipartite interface that is almost indistinguishable from that in Bub3 (Ren et al., 2010).”
SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98 (2021, background): “ent with Rae1 and Nup98 being highly conserved across eukaryotes (6).”
Complexes of Vesicular Stomatitis Virus Matrix Protein with Host Rae1 and Nup98 Involved in Inhibition of Host Transcription (2012, background): “propellers with extensive surface loops [42], which provide large surface areas that could serve as interacting regions for M protein”
Overexpression of SARS-CoV-2 protein ORF6 dislocates RAE1 and NUP98 from the nuclear pore complex (2020, unknown): “heterogeneous ribonucleoprotein A1 (hnRNPA1) relocalization in a RAE1-dependent manner; hnRNPs are thought to serve as mRNA export factors [21,22].”
Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1•Nup98) (2014, background): “The previously reported structures of either M protein (19) or the 1:1 Rae•Nup98 heterodimer (12) are not significantly altered when these reactants associate with each Fig.”
SARS-CoV-2 ORF6 disrupts nucleocytoplasmic transport through interactions with Rae1 and Nup98 (2020, background): “Nup98 is a component of the nuclear pore complex and interacts with the RNA 58 export factor Rae1 to bind single stranded RNA and facilitate the translocation of mRNA 59 through the nuclear pore complex (9, 10).”
Molecular mechanism underlying selective inhibition of mRNA nuclear export by herpesvirus protein ORF10 (2020, background): “The positively charged groove that both ORF10 and the M protein bind in has been reported to be the singlestranded RNA (ssRNA) binding region of Rae1–Nup98 (17, 23), and the formation of the M–Rae1–Nup98 ternary complex disrupts its RNA-binding ability (23).”
Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1–Nup98 Complex to Compete With mRNA Nuclear Export (2022, methodology): “, 2007) using the coordinates of Rae1–Nup98 (PDB ID 3MMY) (Ren et al., 2010) as the search model.”