Karyopherin-independent spontaneous transport of amphiphilic proteins through the nuclear pore
http://www.ncbi.nlm.nih.gov –
Highly selective nucleocytoplasmic molecular transport is critical to eukaryotic cells, which is illustrated by the size-filtering diffusion and karyopherin-mediated passage mechanisms. However, a considerable number of large proteins without nuclear localization signals are localized to the nucleus. Here, we provide evidence for spontaneous migration of large proteins in a karyopherin-independent manner. Time-lapse observation of nuclear transport assay revealed that several large molecules spontaneously and independently pass through the NPC. Read more »
A nuclear export sequence in GPN-loop GTPase 1, an essential protein for nuclear targeting...is necessary and sufficient for nuclear export
http://www.ncbi.nlm.nih.gov –
XAB1/Gpn1 is a GTPase that associates with RNA polymerase II (RNAPII) in a GTP-dependent manner. Although XAB1/Gpn1 is essential for nuclear accumulation of RNAPII, the underlying mechanism is not known. A XAB1/Gpn1-EYFP fluorescent protein, like endogenous XAB1/Gpn1, localized to the cytoplasm but it rapidly accumulated in the cell nucleus in the presence of leptomycin B, a chemical inhibitor of the nuclear transport receptor Crm1. Crm1 recognizes short peptides in substrate proteins called nuclear export sequences (NES). Read more »
Year of publication:
2012
Journal name:
Biochimica et Biophysica Acta (BBA)
Translocation through the nuclear pore: Kaps pave the way
http://www.ncbi.nlm.nih.gov –
Transport through the nuclear pore complex (NPC), a keystone of the eukaryotic building plan, is known to involve a large channel and an abundance of phenylalanine–glycine (FG) protein domains serving as binding sites for soluble nuclear transport receptors and their cargo complexes. However, the conformation of the FG domains in vivo, their arrangement in relation to the transport channel and their function(s) in transport are still vividly debated. Read more »

Category: Nuclear Pore Complex Tags:
Structural biology of nucleocytoplasmic transport.
http://www.ncbi.nlm.nih.gov –
In eukaryotic cells, segregation of DNA replication and RNA biogenesis in the nucleus and protein synthesis in the cytoplasm poses the requirement of transporting thousands of macromolecules between the two cellular compartments. Transport between nucleus and cytoplasm is mediated by soluble receptors that recognize specific cargoes and carry them through the nuclear pore complex (NPC), the sole gateway between the two compartments at interphase. Read more »
Year of publication:
2007
Journal name:
Annual Reviews Biochemistry

Category: Nuclear Pore Complex Tags:
Nuclear Pore Complex: Biochemistry and Biophysics of Nucleocytoplasmic Transport in Health and Disease
http://biomechanics.berkeley.edu –
Nuclear pore complexes (NPCs) are the gateways connecting the nucleoplasm and cytoplasm. This structures are composed of over 30 different proteins and 60–125 MDa of mass depending on type of species. NPCs are bilateral pathways that selectively control the passage of macromolecules into and out of the nucleus. Molecules smaller than 40 kDa diffuse through the NPC passively while larger molecules require facilitated transport provided by their attach- ment to karyopherins. Kinetic studies have shown that approximately 1000 translocations occur per second per NPC. Read more »

Category: Nuclear Pore Complex Tags:
The nuclear pore complex: mediator of translocation between nucleus and cytoplasm.
http://www.ncbi.nlm.nih.gov –
The enclosure of nuclear contents in eukaryotes means that cells require sites in the boundary that mediate exchange of material between nucleus and cytoplasm. These sites, termed nuclear pore complexes (NPCs), number 100-200 in yeast, a few thousand in mammalian cells and approximately 50 million in the giant nuclei of amphibian oocytes. NPCs are large (125 MDa) macromolecular complexes that comprise 50-100 different proteins in vertebrates. In spite of their size and complex structure, NPCs undergo complete breakdown and reformation at cell division. Read more »

Category: Nuclear Pore Complex Tags:
The effects of osmotic stress on the structure and function of the cell nucleus.
http://www.ncbi.nlm.nih.gov –
Osmotic stress is a potent regulator of the normal function of cells that are exposed to osmotically active environments under physiologic or pathologic conditions. The ability of cells to alter gene expression and metabolic activity in response to changes in the osmotic environment provides an additional regulatory mechanism for a diverse array of tissues and organs in the human body. In addition to the activation of various osmotically- or volume-activated ion channels, osmotic stress may also act on the genome via a direct biophysical pathway. Read more »
Year of publication:
2009
Journal name:
J. Cell. Biochem
The molecular architecture of the nuclear pore complex
http://www.nature.com –
Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPC’s 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. Read more »
Year of publication:
2007
Journal name:
Nature
Cryo-electron Tomography Provides Novel Insights into Nuclear Pore Architecture: Implications for Nucleocytoplasmic Transport
http://www.sciencedirect.com –
To go beyond the current structural consensus model of the nuclear pore complex (NPC), we performed cryo-electron tomography of fully native NPCs from Xenopus oocyte nuclear envelopes (NEs). The cytoplasmic face of the NPC revealed distinct anchoring sites for the cytoplasmic filaments, whereas the nuclear face was topped with a massive distal ring positioned above the central pore with indications of the anchoring sites for the nuclear basket filaments and putative intranuclear filaments. Read more »
Year of publication:
2003
Journal name:
Journal of Molecular Biology
Structural analysis of the nuclear pore complex by integrated approaches (Current Opinion in Structural Biology, 2009)
http://www.sciencedirect.com –
In eukaryotic cells, the nucleus is surrounded by a double membrane system, the nuclear envelope (NE), in which the outer membrane is continuous with the endoplasmic reticulum (ER). Nuclear pore complexes (NPCs) fuse the inner and outer nuclear membranes to form aqueous translocation channels that allow the free diffusion of small molecules and ions, as well as receptor-mediated transport of large macromolecules. Read more »
Year of publication:
2009
Journal name:
Current Opinion in Structural Biology

Category: Nuclear Pore Complex Tags:
