Literature DB >> 8740526

Molecular dissection of the nuclear pore complex.

N Panté1, U Aebi.   

Abstract

The nuclear pore complex (NPC) is an approximately 120 megadalton (MDa) supramolecular assembly embedded in the double-membraned nuclear envelope (NE) that mediates bidirectional molecular trafficking between the cytoplasm and the nucleus of interphase eukaryotic cells. The structure of the NPC has been studied extensively by electron microscopy (EM), and a consensus model of its basic framework has emerged. Over the past few years, there has been significant progress in dissecting the molecular constituents of the NPC and in identifying distinct NPC subcomplexes. The combination of well-characterized antibodies with different EM specimen preparation methods has allowed localization of several of these proteins within the three-dimensional (3-D) architecture of the NPC. Thus, the molecular dissection of the NPC is definitely on its way to being elucidated. Here, we review these findings and discuss the emerging structural concepts.

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Year:  1996        PMID: 8740526     DOI: 10.3109/10409239609106583

Source DB:  PubMed          Journal:  Crit Rev Biochem Mol Biol        ISSN: 1040-9238            Impact factor:   8.250


  32 in total

1.  The direction of transport through the nuclear pore can be inverted.

Authors:  M V Nachury; K Weis
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

Review 2.  Transport into and out of the nucleus.

Authors:  I G Macara
Journal:  Microbiol Mol Biol Rev       Date:  2001-12       Impact factor: 11.056

3.  Quantitative topographical analysis of nuclear pore complex function using scanning force microscopy.

Authors:  Rainer D Jäggi; Alfredo Franco-Obregón; Klaus Ensslin
Journal:  Biophys J       Date:  2003-12       Impact factor: 4.033

4.  Regulation of nuclear pore complex conformation by IP(3) receptor activation.

Authors:  David Moore-Nichols; Anne Arnott; Robert C Dunn
Journal:  Biophys J       Date:  2002-09       Impact factor: 4.033

5.  Divalproex sodium modulates nuclear localization of ataxin-3 and prevents cellular toxicity caused by expanded ataxin-3.

Authors:  Zi-Jian Wang; Aoife Hanet; Daniel Weishäupl; Inês M Martins; Anna S Sowa; Olaf Riess; Thorsten Schmidt
Journal:  CNS Neurosci Ther       Date:  2018-01-09       Impact factor: 5.243

6.  Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells.

Authors:  Peter Wild; Monika Engels; Claudia Senn; Kurt Tobler; Urs Ziegler; Elisabeth M Schraner; Eva Loepfe; Mathias Ackermann; Martin Mueller; Paul Walther
Journal:  J Virol       Date:  2005-01       Impact factor: 5.103

7.  From the trap to the basket: getting to the bottom of the nuclear pore complex.

Authors:  Roderick Y H Lim; Ueli Aebi; Daniel Stoffler
Journal:  Chromosoma       Date:  2006-01-10       Impact factor: 4.316

8.  Regulation of NT-PGC-1alpha subcellular localization and function by protein kinase A-dependent modulation of nuclear export by CRM1.

Authors:  Ji Suk Chang; Peter Huypens; Yubin Zhang; Chelsea Black; Anastasia Kralli; Thomas W Gettys
Journal:  J Biol Chem       Date:  2010-03-29       Impact factor: 5.157

9.  A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly.

Authors:  M Bucci; S R Wente
Journal:  Mol Biol Cell       Date:  1998-09       Impact factor: 4.138

10.  Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans.

Authors:  Merav Cohen; Naomi Feinstein; Katherine L Wilson; Yosef Gruenbaum
Journal:  Mol Biol Cell       Date:  2003-07-11       Impact factor: 4.138

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