| Structural highlights
3tkn is a 9 chain structure with sequence from Atcc 18824 and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Gene: | HRB187, J1135, NUP82, YJL061W (ATCC 18824), NUP158, NUP159, RAT7, YIL115C (ATCC 18824), Nup98 (LK3 transgenic mice) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[NUP82_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. It is specifically involved as part of the NUP82-NUP159-NSP1 subcomplex in nuclear mRNA and pre-ribosome export by acting as a linker tethering nucleoporins that are directly involved in nuclear transport to the NPC via its coiled-coil domain.[1] [2] [3] [4] [5] [6] [NUP98_MOUSE] Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC (By similarity). [NU159_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. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.[7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19]
Publication Abstract from PubMed
The cytoplasmic filament nucleoporins of the nuclear pore complex (NPC) are critically involved in nuclear export and remodeling of mRNA ribonucleoprotein particles and are associated with various human malignancies. Here, we report the crystal structure of the Nup98 C-terminal autoproteolytic domain, frequently missing from leukemogenic forms of the protein, in complex with the N-terminal domain of Nup82 and the C-terminal tail fragment of Nup159. The Nup82 beta propeller serves as a noncooperative binding platform for both binding partners. Interaction of Nup98 with Nup82 occurs through a reciprocal exchange of loop structures. Strikingly, the same Nup98 groove promiscuously interacts with Nup82 and Nup96 in a mutually excusive fashion. Simultaneous disruption of both Nup82 interactions in yeast causes severe defects in mRNA export, while the severing of a single interaction is tolerated. Thus, the cytoplasmic filament network of the NPC is robust, consistent with its essential function in nucleocytoplasmic transport.
Molecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore Complex.,Stuwe TT, von Borzyskowski LS, Davenport AM, Hoelz A J Mol Biol. 2012 Apr 2. PMID:22480613[20]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grandi P, Emig S, Weise C, Hucho F, Pohl T, Hurt EC. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J Cell Biol. 1995 Sep;130(6):1263-73. PMID:7559750
- ↑ Belgareh N, Snay-Hodge C, Pasteau F, Dagher S, Cole CN, Doye V. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell. 1998 Dec;9(12):3475-92. PMID:9843582
- ↑ Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000 Aug 4;275(31):23540-8. PMID:10801828 doi:http://dx.doi.org/10.1074/jbc.M001963200
- ↑ Ho AK, Shen TX, Ryan KJ, Kiseleva E, Levy MA, Allen TD, Wente SR. Assembly and preferential localization of Nup116p on the cytoplasmic face of the nuclear pore complex by interaction with Nup82p. Mol Cell Biol. 2000 Aug;20(15):5736-48. PMID:10891509
- ↑ Gleizes PE, Noaillac-Depeyre J, Leger-Silvestre I, Teulieres F, Dauxois JY, Pommet D, Azum-Gelade MC, Gas N. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J Cell Biol. 2001 Dec 10;155(6):923-36. Epub 2001 Dec 10. PMID:11739405 doi:http://dx.doi.org/10.1083/jcb.200108142
- ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
- ↑ Hurwitz ME, Strambio-de-Castillia C, Blobel G. Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex. Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11241-5. PMID:9736720
- ↑ Belgareh N, Snay-Hodge C, Pasteau F, Dagher S, Cole CN, Doye V. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell. 1998 Dec;9(12):3475-92. PMID:9843582
- ↑ Seedorf M, Damelin M, Kahana J, Taura T, Silver PA. Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol. 1999 Feb;19(2):1547-57. PMID:9891088
- ↑ Hodge CA, Colot HV, Stafford P, Cole CN. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 1999 Oct 15;18(20):5778-88. PMID:10523319 doi:10.1093/emboj/18.20.5778
- ↑ Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J Biol Chem. 2000 Aug 4;275(31):23540-8. PMID:10801828 doi:http://dx.doi.org/10.1074/jbc.M001963200
- ↑ Strasser K, Bassler J, Hurt E. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J Cell Biol. 2000 Aug 21;150(4):695-706. PMID:10952996
- ↑ Allen NP, Huang L, Burlingame A, Rexach M. Proteomic analysis of nucleoporin interacting proteins. J Biol Chem. 2001 Aug 3;276(31):29268-74. Epub 2001 May 31. PMID:11387327 doi:http://dx.doi.org/10.1074/jbc.M102629200
- ↑ Gleizes PE, Noaillac-Depeyre J, Leger-Silvestre I, Teulieres F, Dauxois JY, Pommet D, Azum-Gelade MC, Gas N. Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J Cell Biol. 2001 Dec 10;155(6):923-36. Epub 2001 Dec 10. PMID:11739405 doi:http://dx.doi.org/10.1083/jcb.200108142
- ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
- ↑ Allen NP, Patel SS, Huang L, Chalkley RJ, Burlingame A, Lutzmann M, Hurt EC, Rexach M. Deciphering networks of protein interactions at the nuclear pore complex. Mol Cell Proteomics. 2002 Dec;1(12):930-46. PMID:12543930
- ↑ Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2450-5. Epub 2003 Feb 25. PMID:12604785 doi:10.1073/pnas.0437902100
- ↑ Strawn LA, Shen T, Shulga N, Goldfarb DS, Wente SR. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol. 2004 Mar;6(3):197-206. Epub 2004 Feb 22. PMID:15039779 doi:10.1038/ncb1097
- ↑ Weirich CS, Erzberger JP, Berger JM, Weis K. The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol Cell. 2004 Dec 3;16(5):749-60. PMID:15574330 doi:10.1016/j.molcel.2004.10.032
- ↑ Stuwe TT, von Borzyskowski LS, Davenport AM, Hoelz A. Molecular Basis for the Anchoring of Proto-Oncoprotein Nup98 to the Cytoplasmic Face of the Nuclear Pore Complex. J Mol Biol. 2012 Apr 2. PMID:22480613 doi:10.1016/j.jmb.2012.03.024
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