» Articles » PMID: 26967283

The Nuclear Pore Complex As a Flexible and Dynamic Gate

Overview
Journal Cell
Publisher Cell Press
Specialty Cell Biology
Date 2016 Mar 12
PMID 26967283
Citations 193
Authors
Affiliations
Soon will be listed here.
Abstract

Nuclear pore complexes (NPCs) perforate the nuclear envelope and serve as the primary transport gates for molecular exchange between nucleus and cytoplasm. Stripping the megadalton complex down to its most essential organizational elements, one can divide the NPC into scaffold components and the disordered elements attached to them that generate a selective barrier between compartments. These structural elements exhibit flexibility, which may hold a clue in understanding NPC assembly and function. Here we review the current status of NPC research with a focus on the functional implications of its structural and compositional heterogeneity.

Citing Articles

The functions of herpesvirus shuttling proteins in the virus lifecycle.

Cao H, Wang M, Cheng A, Tian B, Yang Q, Ou X Front Microbiol. 2025; 16:1515241.

PMID: 39973925 PMC: 11837949. DOI: 10.3389/fmicb.2025.1515241.


Structures and mRNP remodeling mechanism of the TREX-2 complex.

Xie Y, Clarke B, Xie D, Mei M, Bhat P, Hill P Structure. 2025; 33(3):566-582.e6.

PMID: 39862860 PMC: 11890942. DOI: 10.1016/j.str.2024.12.019.


RRM1 promotes homologous recombination and radio/chemo-sensitivity via enhancing USP11 and E2F1-mediated RAD51AP1 transcription.

Yang S, Wang R, Liu L, Xu F, Zhao X, Yao Z Cell Death Discov. 2024; 10(1):496.

PMID: 39695160 PMC: 11655868. DOI: 10.1038/s41420-024-02267-x.


Nanoscale interactions of arginine-containing dipeptide repeats with nuclear pore complexes as measured by transient scanning electrochemical microscopy.

Huang S, Parandhaman M, Jyothi Ravi M, Janda D, Amemiya S Chem Sci. 2024; .

PMID: 39246336 PMC: 11375788. DOI: 10.1039/d4sc05063k.


An intranuclear bacterial parasite of deep-sea mussels expresses apoptosis inhibitors acquired from its host.

Porras M, Assie A, Tietjen M, Violette M, Kleiner M, Gruber-Vodicka H Nat Microbiol. 2024; 9(11):2877-2891.

PMID: 39242818 PMC: 11521996. DOI: 10.1038/s41564-024-01808-5.


References
1.
Liu X, Mitchell J, Wozniak R, Blobel G, Fan J . Structural evolution of the membrane-coating module of the nuclear pore complex. Proc Natl Acad Sci U S A. 2012; 109(41):16498-503. PMC: 3478598. DOI: 10.1073/pnas.1214557109. View

2.
Schooley A, Vollmer B, Antonin W . Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation. Chromosoma. 2012; 121(6):539-54. PMC: 3501164. DOI: 10.1007/s00412-012-0388-3. View

3.
Capelson M, Liang Y, Schulte R, Mair W, Wagner U, Hetzer M . Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell. 2010; 140(3):372-83. PMC: 2821818. DOI: 10.1016/j.cell.2009.12.054. View

4.
Ori A, Banterle N, Iskar M, Andres-Pons A, Escher C, Khanh Bui H . Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines. Mol Syst Biol. 2013; 9:648. PMC: 3619942. DOI: 10.1038/msb.2013.4. View

5.
Yang W, Gelles J, Musser S . Imaging of single-molecule translocation through nuclear pore complexes. Proc Natl Acad Sci U S A. 2004; 101(35):12887-92. PMC: 516490. DOI: 10.1073/pnas.0403675101. View