| Structural highlights
Function
NU170_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addition it is required for chromosome transmission fidelity.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Nuclear pore complexes (NPCs) direct the nucleocytoplasmic transport of macromolecules. Here, we provide a composite multiscale structure of the yeast NPC, based on improved 3D density maps from cryogenic electron microscopy and AlphaFold2 models. Key features of the inner and outer rings were integrated into a comprehensive model. We resolved flexible connectors that tie together the core scaffold, along with equatorial transmembrane complexes and a lumenal ring that anchor this channel within the pore membrane. The organization of the nuclear double outer ring reveals an architecture that may be shared with ancestral NPCs. Additional connections between the core scaffold and the central transporter suggest that under certain conditions, a degree of local organization is present at the periphery of the transport machinery. These connectors may couple conformational changes in the scaffold to the central transporter to modulate transport. Collectively, this analysis provides insights into assembly, transport, and NPC evolution.
Implications of a multiscale structure of the yeast nuclear pore complex.,Akey CW, Echeverria I, Ouch C, Nudelman I, Shi Y, Wang J, Chait BT, Sali A, Fernandez-Martinez J, Rout MP Mol Cell. 2023 Sep 21;83(18):3283-3302.e5. doi: 10.1016/j.molcel.2023.08.025. PMID:37738963[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marelli M, Aitchison JD, Wozniak RW. Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J Cell Biol. 1998 Dec 28;143(7):1813-30. PMID:9864357
- ↑ Lusk CP, Makhnevych T, Marelli M, Aitchison JD, Wozniak RW. Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. J Cell Biol. 2002 Oct 28;159(2):267-78. Epub 2002 Oct 28. PMID:12403813 doi:10.1083/jcb.200203079
- ↑ Makhnevych T, Lusk CP, Anderson AM, Aitchison JD, Wozniak RW. Cell cycle regulated transport controlled by alterations in the nuclear pore complex. Cell. 2003 Dec 26;115(7):813-23. PMID:14697200
- ↑ Kerscher O, Hieter P, Winey M, Basrai MA. Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation. Genetics. 2001 Apr;157(4):1543-53. PMID:11290711
- ↑ Iouk T, Kerscher O, Scott RJ, Basrai MA, Wozniak RW. The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J Cell Biol. 2002 Dec 9;159(5):807-19. Epub 2002 Dec 9. PMID:12473689 doi:10.1083/jcb.200205068
- ↑ Akey CW, Echeverria I, Ouch C, Nudelman I, Shi Y, Wang J, Chait BT, Sali A, Fernandez-Martinez J, Rout MP. Implications of a multiscale structure of the yeast nuclear pore complex. Mol Cell. 2023 Sep 21;83(18):3283-3302.e5. PMID:37738963 doi:10.1016/j.molcel.2023.08.025
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