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Biology subjects

Woo, T.-T.

Publications and source records attributed to Woo, T.-T..

2 recordsLinked to original sources

Golgi-associated nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection

During human papillomavirus (HPV) entry, the virus exploits COPI-dependent retrograde transport to cross the trans-Golgi network and Golgi stacks before reaching the nucleus to cause infection. How HPV enters the nucleus after exiting the Golgi is unclear, although mitotic nuclear envelop breakdown (NEB) appears important. Here we show that importin-7 (IPO7), a nuclear pore import receptor, associates with the Golgi and promotes HPV infection. Upon IPO7 knockdown, HPV infection is inhibited and the virus accumulates in the Golgi but does not enter the nucleus, demonstrating that IPO7 promotes Golgi-to-nucleus transport of HPV. We further reveal that the C-terminus of HPV capsid protein L2, which is thought to contain overlapping nuclear localization and cell-penetrating peptide sequences, binds directly to IPO7 in a step that requires COPI-dependent virus trafficking. Together these data identify a role of an importin in HPV infection, raising the possibility that the canonical nuclear pore import machinery plays an unanticipated role in NEB-dependent nuclear entry. TeaserHPV, a cancer-causing human pathogen, exploits the Golgi-associated nuclear import receptor IPO7 for Golgi-to-nucleus trafficking to promote infection.

cell biology↗

Intrinsic disorder codes for leaps of protein expression

Serine(S)/threonine(T)-glutamine(Q) cluster domains (SCDs), polyglutamine (polyQ) tracts and polyglutamine/asparagine (polyQ/N) tracts are Q-rich motifs found in many proteins. SCDs often are intrinsically disordered regions that mediate protein phosphorylation and protein-protein interactions. PolyQ and polyQ/N tracts are structurally flexible sequences that trigger protein aggregation. We report that due to their high percentages of STQ or STQN amino acid content, four SCDs and three prion-causing Q/N-rich motifs of yeast proteins possess autonomous protein expression-enhancing activities. Since these Q-rich motifs can endow proteins with structural and functional plasticity, we suggest that they represent useful toolkits for evolutionary novelty. Comparative Gene Ontology (GO) analyses of the near-complete proteomes of 27 representative model eukaryotes reveal that Q-rich motifs prevail in proteins involved in specialized biological processes, including Saccharomyces cerevisiae RNA-mediated transposition and pseudohyphal growth, Candida albicans filamentous growth, ciliate peptidyl-glutamic acid modification and microtubule-based movement, Tetrahymena thermophila xylan catabolism and meiosis, Dictyostelium discoideum development and sexual cycles, Plasmodium falciparum infection, and the nervous systems of Drosophila melanogaster, Mus musculus and Homo sapiens. We also show that Q-rich-motif proteins are expanded massively in ten ciliates with reassigned TAAQ and TAGQ codons. Notably, the usage frequency of CAGQ is much lower in ciliates with reassigned TAAQ and TAGQ codons than in organisms with expanded and unstable Q runs (e.g., D. melanogaster and H. sapiens), indicating that the use of noncanonical stop codons in ciliates may have coevolved with codon usage biases to avoid triplet repeat disorders mediated by CAG/GTC replication slippage.

biochemistry↗