Structural highlights
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Disease
[NUP62_HUMAN] Familial infantile bilateral striatal necrosis. The disease is caused by mutations affecting the gene represented in this entry. [NU155_HUMAN] Familial atrial fibrillation. The disease is caused by mutations affecting the gene represented in this entry.
Function
[NUP62_HUMAN] Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. [NUP54_HUMAN] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. [NU155_HUMAN] Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.[UniProtKB:Q99P88] [NU205_HUMAN] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor NUP62 and other nucleoporins, but not NUP153 and TPR, to the NPC.[1] [NUP93_HUMAN] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. May anchor nucleoporins, but not NUP153 and TPR, to the NPC.[2] [3] [NUP58_HUMAN] Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
Publication Abstract from PubMed
Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.
Molecular architecture of the inner ring scaffold of the human nuclear pore complex.,Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M Science. 2016 Apr 15;352(6283):363-5. doi: 10.1126/science.aaf0643. PMID:27081072[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krull S, Thyberg J, Bjorkroth B, Rackwitz HR, Cordes VC. Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Mol Biol Cell. 2004 Sep;15(9):4261-77. Epub 2004 Jun 30. PMID:15229283 doi:http://dx.doi.org/10.1091/mbc.E04-03-0165
- ↑ Krull S, Thyberg J, Bjorkroth B, Rackwitz HR, Cordes VC. Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Mol Biol Cell. 2004 Sep;15(9):4261-77. Epub 2004 Jun 30. PMID:15229283 doi:http://dx.doi.org/10.1091/mbc.E04-03-0165
- ↑ Hawryluk-Gara LA, Shibuya EK, Wozniak RW. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol Biol Cell. 2005 May;16(5):2382-94. Epub 2005 Feb 9. PMID:15703211 doi:10.1091/mbc.E04-10-0857
- ↑ Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M. Molecular architecture of the inner ring scaffold of the human nuclear pore complex. Science. 2016 Apr 15;352(6283):363-5. doi: 10.1126/science.aaf0643. PMID:27081072 doi:http://dx.doi.org/10.1126/science.aaf0643
