High impact information on NIC96

• There, Nup188p interacts with an integral protein of the pore membrane domain, Pom152p, and another abundant nucleoporin, Nic96p [1].
• The amino-terminal domain of Nic96p physically interacts with the Nsp1p complex which is involved in nucleocytoplasmic transport [2].
• Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p [2].
• Here we show that thermosensitive mutations mapping in the central domain of Nic96p inhibit nuclear pore formation at the nonpermissive temperature [2].
• The NIC96 gene was cloned; it encodes a novel 839 amino acid protein essential for cell growth [3].

Biological context of NIC96

• To more specifically explore the potential role of Nic96p in nuclear protein import, we performed a two-hybrid screen with NIC96 as the bait against a yeast genomic library to identify transport factors and/or nucleoporins involved in nuclear protein import interacting with Nic96p [4].

Anatomical context of NIC96

• By immunofluorescence, protein A-tagged NIC96 exhibits a punctate nuclear membrane staining indicative of nuclear pore location [3].
• When Nic96p was affinity purified from glutaraldehyde-treated spheroplasts, it was found to be associated with Mlp2p [5].

Physical interactions of NIC96

• Purification of NSP1 reveals complex formation with 'GLFG' nucleoporins and a novel nuclear pore protein NIC96 [3].
• The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import [4].
• The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96 [6].

Other interactions of NIC96

• In addition, the synthetic lethal screen identified genetic interactions between Pom152p and two other major nucleoporins, Nup188p (Nehrbass, U., S. Maguire, M. Rout, G. Blobel, and R. W. Wozniak, manuscript submitted for publication), and Nic96p (Grandi, P., V. Doye, and E. C. Hurt. 1993. EMBO J. 12: 3061-71) [7].
• With regard to genetic specificity, the nup116-C lethality was also suppressed by high-copy GLE2 and NIC96 [8].
• Conversely, affinity purification of tagged NSP49 enriches for NSP1, the p54 and the NIC96 component [3].
• The requirement for Pom152p in strains containing mutations allelic to the NPC protein genes NIC96 and NUP59 could be alleviated by Pom152p's N terminus, independent of its integration into the membrane [9].
• Here we report the analysis of strains mutant in either of two nucleoporin-encoding genes, NIC96 (Zabel et al., 1996) and NUP192 (Kosova et al., 1999) [10].

Analytical, diagnostic and therapeutic context of NIC96

• Immunoprecipitation from both mammalian and Xenopus cell extracts indicates that a small fraction of Nup93 physically interacts with the nucleoporin p62, just as yeast Nic96p interacts with the yeast p62 homologue [11].
• Sequence analysis indicated that the homology of the rice field eel Nup93 were 36.5% with yeast Nic96, 94.6% and 90.5% with Nup93 of zebrafish and human, respectively [12].

References