The movement of proteins between the cytoplasm and nucleus mediated by the importin superfamily of proteins is essential to many cellular processes, including differentiation and development, and is critical to disease states such as viral disease and oncogenesis We recently developed a high-throughput screen to identify specific and general inhibitors of protein nuclear import, from which ivermectin was identified as a potential inhibitor of importin α/β-mediated transport In the present study, we characterized in detail the nuclear transport inhibitory properties of ivermectin, demonstrating that it is a broad-spectrum inhibitor of importin α/β nuclear import, with no effect on a range of other nuclear import pathways, including that mediated by importin β1 alone Importantly, we establish for the first time that ivermectin has potent antiviral activity towards both HIV-1 and dengue virus, both of which are strongly reliant on importin α/β nuclear import, with respect to the HIV-1 integrase and NS5 (non-structural protein 5) polymerase proteins respectively Ivermectin would appear to be an invaluable tool for the study of protein nuclear import, as well as the basis for future development of antiviral agents

/pdf/ivermectin-is-a-specific-inhibitor-of-importin-a-b-mediated-1b0gno3h89.pdf

Ivermectin is a specific inhibitor of importin α/β-mediated nuclear import able to inhibit replication of HIV-1 and dengue virus.

In the year 2003 there was a 17% increase in the number of publications citing work performed using optical biosensor technology compared with the previous year. We collated the 962 total papers for 2003, identified the geographical regions where the work was performed, highlighted the instrument types on which it was carried out, and segregated the papers by biological system. In this overview, we spotlight 13 papers that should be on everyone's 'must read' list for 2003 and provide examples of how to identify and interpret high-quality biosensor data. Although we still find that the literature is replete with poorly performed experiments, over-interpreted results and a general lack of understanding of data analysis, we are optimistic that these shortcomings will be addressed as biosensor technology continues to mature.

https://onlinelibrary.wiley.com/doi/pdf/10.1002/jmr.753

Survey of the year 2003 commercial optical biosensor literature

http://biology.hunter.cuny.edu/cellbio/Feinstein%20Cell%20Bio%202013/Zhong/interesting%20papers/Dynamics%20of%20NPCs%20Tran%20&%20Wente%20Cell2006.pdf

Dynamic Nuclear Pore Complexes: Life on the Edge

http://web.clas.ufl.edu/users/msscha/bioreview/nuclear_pore_complexes.pdf

Structure, dynamics and function of nuclear pore complexes.

The etiology of PNSTs is usually unknown. However, several hereditary disorders are known to predispose to benign and malignant PNSTs, notably neurofibromatosis type 1 (NF1) and neurofibromatosis type 2 (NF2), both of which are inherited in an autosomal dominant fashion. NF1 (also known as von Recklinghausen disease) is caused by mutations in the NF1 gene on chromosome 17 and is characterized by several phenotypic features including multiple neurofibromas and MPNSTs. The incidence of MPNST is in general rare, but half of all cases arise in NF1 patients. NF2, caused by mutations in the NF2 gene on chromosome 22, predisposes to schwannomas, predominantly affecting the spine and the intracranial nerves.

Atlas of Genetics and Cytogenetics in Oncology and Haematology

A 1933 bp cDNA fragment, coding a truncated testis-specific novel nucleoporin, was isolated from a human testis λZAPII cDNA library, designated as BS-63 and assigned GenBank accession number: U64675. By applying the methods of rapid amplification of cDNA ends (5′ RACE) and PCR, a full-length BS-63 cDNA composed of 5475 bp was obtained. BS-63 cDNA contained an open reading frame consisting of 1765 codons and XFXFG or GLFG repetitive sequence motifs. These repetitive motifs are structural characteristic of nucleoporins. BS-63 cDNA has high homology with Nup358/Ran BP2. A 1599 bp fragment, corresponding to the C-terminus of BS-63 cDNA, was prepared and expressed in E. coli BL21(DE3). The recombinant product was purified by affinity chromatography and SDS–PAGE and polyclonal antibodies raised. In rat testis section, the BS-63 protein was localized at the sites of nuclear pores in spermatids by immuno-gold transmission electron microscopy and on the nuclear membrane of Triton X-treated sperm by colloidal silver immuno-gold scanning electron microscopy. The recombinant BS-63 protein can be phosphorylated in vitro with PKC and p34cdc2. A yeast two-hybrid system was used to screen a mouse testis cDNA library to identify proteins capable of interacting with BS-63. Using the 1.6 kb cDNA fragment as bait, the following interacting proteins were identified: Ran, transportin (karyopherin beta2), two proteins related to the nucleocytoplasmic transporter and aF10 protein. The latter protein is a putative transcriptor containing a cysteine-rich N-terminus, a LAP/PHD finger, a leucine zipper domain and a glutamine-rich C-terminus. Also it is highly expressed in murine testis and is located in the cell nucleus and cytoplasm. The interaction of BS-63 with aF10 (696–1001aa) was validated by surface plasmon resonance and by affinity precipitation combined with Western blot. aF10 (696–1001aa) interacted in vitro with BS-63 extracted from rat testis germ cells. It is hypothesized that BS-63 is a testis-specific nucleoporin and possibly acts as a docking site and a cotransporter of Ran and transportin. The complex performs the task of a carrier system in transporting aF10 into the nucleus of germ cells during spermiogenesis. Mol. Reprod. Dev. 61: 126–134, 2002. © 2002 Wiley-Liss, Inc.

Characterization and potential function of a novel testis-specific nucleoporin BS-63.

hSMP-1 is a human sperm membrane protein expressed during development. It is a testis-specific component produced during male germ cell differentiation. Proteins that interact with hSMP-1 were identified by the application of the yeast two-hybrid system. One of the components, RanBPM, was found to be associated with hSMP-1 under both in vitro and in vivo conditions. In the human testis, RanBPM is produced in spermatogonia and primary spermatocytes, suggesting expression during the early stages of spermatogenesis; whereas in the rat testis, it is located in round and elongated spermatids, similar to hSMP-1, suggesting expression of both components during spermiogenesis. Images obtained by immunofluorescence and confocal scanning microscopy of CHO-K1 cells co-transfected with pEGFP-C1-hSMP-1 and pDsRed1-Nl-RanBPM revealed that RanBPM and hSMP-1 are distributed in discrete loci throughout the cytoplasm. When superimposed, the stained spots appeared as congruent yellow areas, indicative of co-localization and probable complex formation of these two components. This interaction between hSMP-1 and RanBPM may be involved in the process of male germ cell differentiation. In CHO-Kl cells transfected with pEGFP-Cl-hSMP-1, the exogenously expressed hSMP-1 was found to co-localize with α-tubulin. Depolymerization of microtubules can be induced in CHO-Kl cells by cold treatment. In cells transfected with the pEGFP-Cl vector, the dispersed tubulins promptly reassembled upon warming. However, in cells transfected with pEGFP-Cl-hSMP-1, reassembly of the dispersed tubulins was blocked even upon rewarming of the cells. These findings suggest that hSMP-1 interacts with tubulins and thereby may modulate microtubule assembly and/or activity.

Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre

This invention relates to biology function of gene coding protein of testis distinguished expression. The gene name is HSD-1, its coding protein name is hSMP-1. HSD-1 is named by human gene naming database as SPAG8. The content includes bait is hSMP-1 albumen, human testis cDNA library is sieved by yeast doublecross method, and then coding cDNA segment of RanBPM is got. Showed by immune group result, RanBPM in human testis tissue is mainly pitched spermatogonium and primary spermatocyte. Then mutual interaction of hSMP-1 and RanBPM albumen is confirmed from in vivo and in vitro two aspects. Showed by cell immune fluorescence result, in CHO-K1 cell, bait albumen and seized albumen show fully same position fixing. Revealed by series researches, hSMP-1 albumen can adjust microtubule activity, take part in mitosis process, and bring changes of cell period. The explanation of its physiological and physiochemical function has great meaning to know gene express, regulation and control rule and origination mechanism of germ cell.

Biology function of encoded protein of HSD-1ú¿SPAG8ú® gene specific for human testis

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Characterization and potential function of a novel testis-specific nucleoporin BS-63.

Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre

Biology function of encoded protein of HSD-1ú¿SPAG8ú® gene specific for human testis