5a9q

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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NUP98_HUMAN NUP98_HUMAN]] Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The FG repeat domains in Nup98 have a direct role in the transport. [[http://www.uniprot.org/uniprot/NUP37_HUMAN NUP37_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.<ref>PMID:17363900</ref> [[http://www.uniprot.org/uniprot/SEC13_HUMAN SEC13_HUMAN]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles.<ref>PMID:8972206</ref> [[http://www.uniprot.org/uniprot/NUP85_HUMAN NUP85_HUMAN]] Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade.<ref>PMID:12718872</ref> <ref>PMID:15995708</ref> <ref>PMID:16807356</ref> [[http://www.uniprot.org/uniprot/NU160_HUMAN NU160_HUMAN]] Involved in poly(A)+ RNA transport.<ref>PMID:11684705</ref> [[http://www.uniprot.org/uniprot/SEH1_HUMAN SEH1_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.<ref>PMID:15146057</ref> <ref>PMID:17363900</ref> <ref>PMID:23723238</ref> [[http://www.uniprot.org/uniprot/NUP43_HUMAN NUP43_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.<ref>PMID:17363900</ref> [[http://www.uniprot.org/uniprot/NU133_HUMAN NU133_HUMAN]] Involved in poly(A)+ RNA transport.<ref>PMID:11684705</ref> [[http://www.uniprot.org/uniprot/NU155_HUMAN 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] [[http://www.uniprot.org/uniprot/NU107_HUMAN NU107_HUMAN]] Essential component of nuclear pore complex. Required for the assembly of peripheral proteins into the nuclear pore complex.<ref>PMID:12552102</ref>
[[http://www.uniprot.org/uniprot/NUP98_HUMAN NUP98_HUMAN]] Nup98 and Nup96 play a role in the bidirectional transport across the nucleoporin complex (NPC). The FG repeat domains in Nup98 have a direct role in the transport. [[http://www.uniprot.org/uniprot/NUP37_HUMAN NUP37_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.<ref>PMID:17363900</ref> [[http://www.uniprot.org/uniprot/SEC13_HUMAN SEC13_HUMAN]] Functions as a component of the nuclear pore complex (NPC) and the COPII coat. At the endoplasmic reticulum, SEC13 is involved in the biogenesis of COPII-coated vesicles.<ref>PMID:8972206</ref> [[http://www.uniprot.org/uniprot/NUP85_HUMAN NUP85_HUMAN]] Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance. As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP98/Nup98 and NUP153 to the nucleus. The Nup107-160 complex seems to be required for spindle assembly during mitosis. NUP85 is required for membrane clustering of CCL2-activated CCR2. Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade.<ref>PMID:12718872</ref> <ref>PMID:15995708</ref> <ref>PMID:16807356</ref> [[http://www.uniprot.org/uniprot/NU160_HUMAN NU160_HUMAN]] Involved in poly(A)+ RNA transport.<ref>PMID:11684705</ref> [[http://www.uniprot.org/uniprot/SEH1_HUMAN SEH1_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore. As a component of the GATOR2 complex, inhibits GATOR1 complex, an inhibitor of the amino acid-sensing branch of the TORC1 pathway.<ref>PMID:15146057</ref> <ref>PMID:17363900</ref> <ref>PMID:23723238</ref> [[http://www.uniprot.org/uniprot/NUP43_HUMAN NUP43_HUMAN]] Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.<ref>PMID:17363900</ref> [[http://www.uniprot.org/uniprot/NU133_HUMAN NU133_HUMAN]] Involved in poly(A)+ RNA transport.<ref>PMID:11684705</ref> [[http://www.uniprot.org/uniprot/NU155_HUMAN 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] [[http://www.uniprot.org/uniprot/NU107_HUMAN NU107_HUMAN]] Essential component of nuclear pore complex. Required for the assembly of peripheral proteins into the nuclear pore complex.<ref>PMID:12552102</ref>
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== Publication Abstract from PubMed ==
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Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approximately 30 nucleoporins (Nups), 15 are structured and form the Y and inner-ring complexes. These two major scaffolding modules assemble in multiple copies into an eight-fold rotationally symmetric structure that fuses the inner and outer nuclear membranes to form a central channel of ~60 nm in diameter. The scaffold is decorated with transport-channel Nups that often contain phenylalanine-repeat sequences and mediate the interaction with cargo complexes. Although the architectural arrangement of parts of the Y complex has been elucidated, it is unclear how exactly it oligomerizes in situ. Here we combine cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate, to our knowledge, the most comprehensive architectural model of the human nuclear pore complex to date. Our data suggest previously unknown protein interfaces across Y complexes and to inner-ring complex members. We show that the transport-channel Nup358 (also known as Ranbp2) has a previously unanticipated role in Y-complex oligomerization. Our findings blur the established boundaries between scaffold and transport-channel Nups. We conclude that, similar to coated vesicles, several copies of the same structural building block--although compositionally identical--engage in different local sets of interactions and conformations.
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In situ structural analysis of the human nuclear pore complex.,von Appen A, Kosinski J, Sparks L, Ori A, DiGuilio AL, Vollmer B, Mackmull MT, Banterle N, Parca L, Kastritis P, Buczak K, Mosalaganti S, Hagen W, Andres-Pons A, Lemke EA, Bork P, Antonin W, Glavy JS, Bui KH, Beck M Nature. 2015 Oct 1;526(7571):140-3. doi: 10.1038/nature15381. Epub 2015 Sep 23. PMID:26416747<ref>PMID:26416747</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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<references/>

Revision as of 21:37, 15 October 2015

Human nuclear pore complex

5a9q, resolution 23.00Å

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