The cellular environment shapes the nuclear pore complex architecture.
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
received:
29
04
2021
accepted:
01
09
2021
pubmed:
15
10
2021
medline:
9
2
2022
entrez:
14
10
2021
Statut:
ppublish
Résumé
Nuclear pore complexes (NPCs) create large conduits for cargo transport between the nucleus and cytoplasm across the nuclear envelope (NE)
Identifiants
pubmed: 34646014
doi: 10.1038/s41586-021-03985-3
pii: 10.1038/s41586-021-03985-3
pmc: PMC8550940
doi:
Substances chimiques
Nuclear Pore Complex Proteins
0
nuclear pore complex protein 96
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
667-671Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM077537
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM141834
Pays : United States
Commentaires et corrections
Type : CommentIn
Type : CommentIn
Informations de copyright
© 2021. The Author(s).
Références
Grossman, E., Medalia, O. & Zwerger, M. Functional architecture of the nuclear pore complex. Annu. Rev. Biophys. 41, 557–584 (2012).
pubmed: 22577827
doi: 10.1146/annurev-biophys-050511-102328
Knockenhauer, K. E. & Schwartz, T. U. The nuclear pore complex as a flexible and dynamic gate. Cell 164, 1162–1171 (2016).
pubmed: 26967283
pmcid: 4788809
doi: 10.1016/j.cell.2016.01.034
Strambio-De-Castillia, C., Niepel, M. & Rout, M. P. The nuclear pore complex: bridging nuclear transport and gene regulation. Nat. Rev. Mol. Cell Biol. 11, 490–501 (2010).
pubmed: 20571586
doi: 10.1038/nrm2928
Hampoelz, B., Andres-Pons, A., Kastritis, P. & Beck, M. Structure and assembly of the nuclear pore complex. Annu. Rev. Biophys. 48, 515–536 (2019).
pubmed: 30943044
doi: 10.1146/annurev-biophys-052118-115308
Lin, D. H. & Hoelz, A. The structure of the nuclear pore complex (an update). Annu. Rev. Biochem. 88, 725–783 (2019).
pubmed: 30883195
pmcid: 6588426
doi: 10.1146/annurev-biochem-062917-011901
Schwartz, T. U. The structure inventory of the nuclear pore complex. J. Mol. Biol. 428, 1986–2000 (2016).
pubmed: 27016207
pmcid: 4886551
doi: 10.1016/j.jmb.2016.03.015
Fernandez-Martinez, J. & Rout, M. P. One ring to rule them all? Structural and functional diversity in the nuclear pore complex. Trends Biochem. Sci. https://doi.org/10.1016/j.tibs.2021.01.003 (2021).
Fernandez-Martinez, J. et al. Structure and function of the nuclear pore complex cytoplasmic mRNA export platform. Cell 167, 1215–1228 (2016).
pubmed: 27839866
pmcid: 5130164
doi: 10.1016/j.cell.2016.10.028
Kosinski, J. et al. Molecular architecture of the inner ring scaffold of the human nuclear pore complex. Science 352, 363–365 (2016).
pubmed: 27081072
doi: 10.1126/science.aaf0643
Kampmann, M. & Blobel, G. Three-dimensional structure and flexibility of a membrane-coating module of the nuclear pore complex. Nat. Struct. Mol. Biol. 16, 782–788 (2009).
pubmed: 19503077
pmcid: 2706296
doi: 10.1038/nsmb.1618
Kelley, K., Knockenhauer, K. E., Kabachinski, G. & Schwartz, T. U. Atomic structure of the Y complex of the nuclear pore. Nat. Struct. Mol. Biol. 22, 425–431 (2015).
pubmed: 25822992
pmcid: 4424061
doi: 10.1038/nsmb.2998
Bui, K. H. et al. Integrated structural analysis of the human nuclear pore complex scaffold. Cell 155, 1233–1243 (2013).
pubmed: 24315095
doi: 10.1016/j.cell.2013.10.055
Lutzmann, M., Kunze, R., Buerer, A., Aebi, U. & Hurt, E. Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J. 21, 387–397 (2002).
pubmed: 11823431
pmcid: 125826
doi: 10.1093/emboj/21.3.387
Stuwe, T. et al. Architecture of the nuclear pore complex coat. Science 347, 1148–1152 (2015).
pubmed: 25745173
pmcid: 5180592
doi: 10.1126/science.aaa4136
von Appen, A. et al. In situ structural analysis of the human nuclear pore complex. Nature 526, 140–143 (2015).
doi: 10.1038/nature15381
Maimon, T., Elad, N., Dahan, I. & Medalia, O. The human nuclear pore complex as revealed by cryo-electron tomography. Structure 20, 998–1006 (2012).
pubmed: 22632834
doi: 10.1016/j.str.2012.03.025
Villa, E., Schaffer, M., Plitzko, J. M. & Baumeister, W. Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography. Curr. Opin. Struct. Biol. 23, 771–777 (2013).
pubmed: 24090931
doi: 10.1016/j.sbi.2013.08.006
Allegretti, M. et al. In-cell architecture of the nuclear pore and snapshots of its turnover. Nature 586, 796–800 (2020).
pubmed: 32879490
doi: 10.1038/s41586-020-2670-5
Zimmerli, C. E. et al. Nuclear pores constrict upon energy depletion. Preprint at https://doi.org/10.1101/2020.07.30.228585 (2020).
Mosalaganti, S. et al. In situ architecture of the algal nuclear pore complex. Nat. Commun. 9, 2361 (2018).
pubmed: 29915221
pmcid: 6006428
doi: 10.1038/s41467-018-04739-y
Mahamid, J. et al. Visualizing the molecular sociology at the HeLa cell nuclear periphery. Science 351, 969–972 (2016).
pubmed: 26917770
doi: 10.1126/science.aad8857
Zila, V. et al. Cone-shaped HIV-1 capsids are transported through intact nuclear pores. Cell 184, 1032–1046 (2021).
pubmed: 33571428
pmcid: 7895898
doi: 10.1016/j.cell.2021.01.025
Regmi, S. G. et al. The nuclear pore complex consists of two independent scaffolds. Preprint at https://doi.org/10.1101/2020.11.13.381947 (2020).
Nordeen, S. A., Turman, D. L. & Schwartz, T. U. Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nat. Commun. 11, 6060 (2020).
pubmed: 33247142
pmcid: 7695694
doi: 10.1038/s41467-020-19885-5
Teimer, R., Kosinski, J., von Appen, A., Beck, M. & Hurt, E. A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex. Nat. Commun. 8, 1107 (2017).
pubmed: 29062044
pmcid: 5653651
doi: 10.1038/s41467-017-01160-9
Eibauer, M. et al. Structure and gating of the nuclear pore complex. Nat. Commun. 6, 7532 (2015).
pubmed: 26112706
doi: 10.1038/ncomms8532
Huang, G. et al. Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis. Cell Res. 30, 520–531 (2020).
pubmed: 32376910
pmcid: 7264146
doi: 10.1038/s41422-020-0319-4
Hulsmann, B. B., Labokha, A. A. & Gorlich, D. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150, 738–751 (2012).
pubmed: 22901806
doi: 10.1016/j.cell.2012.07.019
Kronenberg-Tenga, R. et al. A lamin A/C variant causing striated muscle disease provides insights into filament organization. J. Cell Sci. 134, jcs256156 (2021).
pubmed: 33536248
doi: 10.1242/jcs.256156
Thaller, D. J. & Lusk, P. C. Fantastic nuclear envelope herniations and where to find them. Biochem. Soc. Trans. 46, 877–889 (2018).
pubmed: 30026368
pmcid: 6195200
doi: 10.1042/BST20170442
Lin, D. H. et al. Architecture of the symmetric core of the nuclear pore. Science 352, aaf1015 (2016).
pubmed: 27081075
pmcid: 5207208
doi: 10.1126/science.aaf1015
Sapra, K. T. et al. Nonlinear mechanics of lamin filaments and the meshwork topology build an emergent nuclear lamina. Nat. Commun. 11, 6205 (2020).
pubmed: 33277502
pmcid: 7718915
doi: 10.1038/s41467-020-20049-8
Turgay, Y. et al. The molecular architecture of lamins in somatic cells. Nature 543, 261–264 (2017).
pubmed: 28241138
pmcid: 5616216
doi: 10.1038/nature21382
Feldherr, C., Akin, D. & Moore, M. S. The nuclear import factor p10 regulates the functional size of the nuclear pore complex during oogenesis. J. Cell Sci. 111, 1889–1896 (1998).
pubmed: 9625751
doi: 10.1242/jcs.111.13.1889
Onischenko, E. et al. Natively unfolded FG repeats stabilize the structure of the nuclear pore complex. Cell 171, 904–917 (2017).
pubmed: 29033133
pmcid: 5992322
doi: 10.1016/j.cell.2017.09.033
Kim, S. J. et al. Integrative structure and functional anatomy of a nuclear pore complex. Nature 555, 475–482 (2018).
pubmed: 29539637
pmcid: 6022767
doi: 10.1038/nature26003
Ungricht, R. & Kutay, U. Establishment of NE asymmetry-targeting of membrane proteins to the inner nuclear membrane. Curr. Opin. Cell Biol. 34, 135–141 (2015).
pubmed: 26112002
doi: 10.1016/j.ceb.2015.04.005
Meinema, A. C. et al. Long unfolded linkers facilitate membrane protein import through the nuclear pore complex. Science 333, 90–93 (2011).
pubmed: 21659568
doi: 10.1126/science.1205741
Frey, S., Richter, R. P. & Gorlich, D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314, 815–817 (2006).
pubmed: 17082456
doi: 10.1126/science.1132516
Frey, S. & Gorlich, D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130, 512–523 (2007).
pubmed: 17693259
doi: 10.1016/j.cell.2007.06.024
Ori, A. et al. Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines. Mol. Syst. Biol. 9, 648 (2013).
pubmed: 23511206
pmcid: 3619942
doi: 10.1038/msb.2013.4
, M. & D’Angelo, M. A. Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions. Nat. Rev. Mol. Cell Biol. 13, 687–699 (2012).
pubmed: 23090414
doi: 10.1038/nrm3461
Demircioglu, F. E. et al. The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. Nat. Commun. 10, 3262 (2019).
pubmed: 31332180
pmcid: 6646356
doi: 10.1038/s41467-019-11194-w
Wagner, F. R. et al. Preparing samples from whole cells using focused-ion-beam milling for cryo-electron tomography. Nat. Protoc. 15, 2041–2070 (2020).
pubmed: 32405053
pmcid: 8053421
doi: 10.1038/s41596-020-0320-x
Hagen, W. J. H., Wan, W. & Briggs, J. A. G. Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging. J. Struct. Biol. 197, 191–198 (2017).
pubmed: 27313000
pmcid: 5287356
doi: 10.1016/j.jsb.2016.06.007
Kremer, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71–76 (1996).
pubmed: 8742726
doi: 10.1006/jsbi.1996.0013
Forster, F., Medalia, O., Zauberman, N., Baumeister, W. & Fass, D. Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography. Proc. Natl Acad. Sci. USA 102, 4729–4734 (2005).
pubmed: 15774580
pmcid: 555690
doi: 10.1073/pnas.0409178102
Beck, M., Lucic, V., Forster, F., Baumeister, W. & Medalia, O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 449, 611–615 (2007).
pubmed: 17851530
doi: 10.1038/nature06170
Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012).
pubmed: 23000701
pmcid: 3690530
doi: 10.1016/j.jsb.2012.09.006
Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
pubmed: 15264254
doi: 10.1002/jcc.20084
Virtanen, P. et al. SciPy 1.0: fundamental algorithms for scientific computing in Python. Nat. Methods 17, 261–272 (2020).
pubmed: 32015543
pmcid: 7056644
doi: 10.1038/s41592-019-0686-2
Seabold, S. & Perktold, J. statsmodels: econometric and statistical modeling with Python. In Proc. 9th Python in Science Conference (2010).
Hunter, J. D. Matplotlib: a 2D graphics environment. Comput. Sci. Eng. 9, 90–95 (2007).
doi: 10.1109/MCSE.2007.55
Nickell, S. et al. TOM software toolbox: acquisition and analysis for electron tomography. J. Struct. Biol. 149, 227–234 (2005).
pubmed: 15721576
doi: 10.1016/j.jsb.2004.10.006