Literature DB >> 12648571

Nuclear pore complexes exceeding eightfold rotational symmetry.

Jenny E Hinshaw1, Ronald A Milligan.   

Abstract

Nuclear pore complexes are rotationally symmetric structures that span the nuclear envelope and provide channels for nucleocytoplasmic traffic. These large complexes normally consist of eight spokes arranged around a central channel, although, occasionally, 9- and 10-fold nuclear pore complexes are found in preparations of Xenopus oocyte macronuclei. Here we examine these unusual nuclear pore complexes by negative stain electron microscopy and image analysis and compare the results with data previously obtained from 8-fold structures. The details in two-dimensional and three-dimensional maps indicate that the substructure of the spoke is the same in 8-, 9- and 10-fold nuclear pore complexes: therefore, the spoke is likely an immutable structural component. In all three variant forms, the spacing between adjacent annular subunits, which surround the central channel, is identical. Distances between spokes at higher radius decrease in the 9- and 10-fold nuclear pore complexes. These data imply that the most important connections holding the nuclear pore complex together are those between adjacent annular subunits and that these interactions may play a predominant role in nuclear pore complex assembly. Circumferential connections mediated by ring subunits and radial arms presumably further stabilize the structure and are flexible enough to accommodate additional spokes.

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Year:  2003        PMID: 12648571     DOI: 10.1016/s1047-8477(02)00626-3

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  17 in total

Review 1.  Nuclear pore biogenesis into an intact nuclear envelope.

Authors:  Christine M Doucet; Martin W Hetzer
Journal:  Chromosoma       Date:  2010-08-19       Impact factor: 4.316

2.  On the octagonal structure of the nuclear pore complex: insights from coarse-grained models.

Authors:  Christopher Wolf; Mohammad R K Mofrad
Journal:  Biophys J       Date:  2008-05-16       Impact factor: 4.033

3.  The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex.

Authors:  Gandhi Theerthagiri; Nathalie Eisenhardt; Heinz Schwarz; Wolfram Antonin
Journal:  J Cell Biol       Date:  2010-06-21       Impact factor: 10.539

Review 4.  Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.

Authors:  Siegfried M Musser; David Grünwald
Journal:  J Mol Biol       Date:  2016-03-02       Impact factor: 5.469

5.  Structural evidence for common ancestry of the nuclear pore complex and vesicle coats.

Authors:  Stephen G Brohawn; Nina C Leksa; Eric D Spear; Kanagalaghatta R Rajashankar; Thomas U Schwartz
Journal:  Science       Date:  2008-10-30       Impact factor: 47.728

6.  NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes.

Authors:  Fabrizia Stavru; Bastian B Hülsmann; Anne Spang; Enno Hartmann; Volker C Cordes; Dirk Görlich
Journal:  J Cell Biol       Date:  2006-05-15       Impact factor: 10.539

7.  Quantifying nucleoporin stoichiometry inside single nuclear pore complexes in vivo.

Authors:  Lan Mi; Alexander Goryaynov; Andre Lindquist; Michael Rexach; Weidong Yang
Journal:  Sci Rep       Date:  2015-03-23       Impact factor: 4.379

Review 8.  Modeling of the mechano-chemical behaviour of the nuclear pore complex: current research and perspectives.

Authors:  Alberto Garcia; Jose F Rodriguez Matas; Manuela T Raimondi
Journal:  Integr Biol (Camb)       Date:  2016-10-10       Impact factor: 2.192

9.  Molecular connections between nuclear and ciliary import processes.

Authors:  H Lynn Kee; Kristen J Verhey
Journal:  Cilia       Date:  2013-08-28

10.  Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex.

Authors:  Mohaddeseh Peyro; Mohammad Soheilypour; Ali Ghavami; Mohammad R K Mofrad
Journal:  PLoS One       Date:  2015-12-11       Impact factor: 3.240

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