NDLI: The nuclear pore complex and nuclear transport.

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The nuclear pore complex and nuclear transport.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wente, Susan R. Rout, Michael P.
Description	Country affiliation: United States Author Affiliation: Wente SR ( Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, Tennessee 37232, USA. susan.wente@vanderbilt.edu)
Abstract	Internal membrane bound structures sequester all genetic material in eukaryotic cells. The most prominent of these structures is the nucleus, which is bounded by a double membrane termed the nuclear envelope (NE). Though this NE separates the nucleoplasm and genetic material within the nucleus from the surrounding cytoplasm, it is studded throughout with portals called nuclear pore complexes (NPCs). The NPC is a highly selective, bidirectional transporter for a tremendous range of protein and ribonucleoprotein cargoes. All the while the NPC must prevent the passage of nonspecific macromolecules, yet allow the free diffusion of water, sugars, and ions. These many types of nuclear transport are regulated at multiple stages, and the NPC carries binding sites for many of the proteins that modulate and modify the cargoes as they pass across the NE. Assembly, maintenance, and repair of the NPC must somehow occur while maintaining the integrity of the NE. Finally, the NPC appears to be an anchor for localization of many nuclear processes, including gene activation and cell cycle regulation. All these requirements demonstrate the complex design of the NPC and the integral role it plays in key cellular processes.
File Format	HTM / HTML
e-ISSN	19430264
DOI	10.1101/cshperspect.a000562
Journal	Cold Spring Harbor Perspectives in Biology
Issue Number	10
Volume Number	2
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2010-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Biology Cell Nucleus Metabolism Eukaryotic Cells Nuclear Pore Complex Proteins Saccharomyces Cerevisiae Biological Transport, Active Ultrastructure Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article

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Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae

The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly

Coordination of tRNA transcription with export at nuclear pore complexes in budding yeast.

ER membrane–bending proteins are necessary for de novo nuclear pore formation

Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae

The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1.

Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.

Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket

A subset of FG-nucleoporins is necessary for efficient Msn5-mediated nuclear protein export.

The nuclear pore complex and nuclear transport.

Similar Documents

Altering nuclear pore complex function impacts longevity and mitochondrial function in S. cerevisiae

The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly

Coordination of tRNA transcription with export at nuclear pore complexes in budding yeast.

ER membrane–bending proteins are necessary for de novo nuclear pore formation

Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae

The Dbp5 cycle at the nuclear pore complex during mRNA export I: dbp5 mutants with defects in RNA binding and ATP hydrolysis define key steps for Nup159 and Gle1.

Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.

Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket

A subset of FG-nucleoporins is necessary for efficient Msn5-mediated nuclear protein export.

The nuclear pore complex and nuclear transport.