Nuclear Pore Function

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Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer

Nuclear pore complexes control trafficking of proteins and RNA in and out of the nucleus. These studies now provide evidence that AD-related tau disrupts nuclear pore function in Alzheimer sdiseaseandthatnuclearpore proteins cause tau to aggregate. Eftekharzadeh et al., 2018, Neuron 99, 925 940 September 5, 2018 ª 2018 Elsevier Inc.

Dynamics of nuclear pore density and distribution patterns

followed vegetative nuclear pore density and distri-bution as it relates to the formation of a close physical association between the VN and the GC. Taken together with biochemical studies on RNA and protein synthesis during pollen development, and studies on nuclear pore function, these results support the notion that even though mean pollen

Gene loops function to maintain transcriptional memory

Gene loops function to maintain transcriptional memory through interaction with the nuclear pore complex Sue Mei Tan-Wong,1 Hashanthi D. Wijayatilake,1 and Nick J. Proudfoot2 Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom

The nuclear pore complex and chromatin boundaries

between the function of boundary and insulator elements and their ability to establish separate chromatin domains. More interestingly, these results suggest that the boundary activity of a DNA sequence depends on its interaction with protein components of the nuclear pore complex (NPC). This nuclear structure, whose role in nuclear physiology

Nuclear Pore Scaffold Structure Analyzed by Super-Resolution

Nuclear Pore Scaffold Structure Analyzed by Super-Resolution Microscopy and Particle Averaging Anna Szymborska,1 Alex de Marco,2 Nathalie Daigle,1 Volker C. Cordes,3 John A. G. Briggs,2 Jan Ellenberg1* Much of life s essential molecular machinery consists of large protein assemblies that currently pose challenges for structure determination.

Mutations in nuclear pore genes

Mutations in nuclear pore genes between the cytoplasm and the nuclear interior. Nucleoporins function by interacting with transport receptors such as

The SUMO proteases SENP1 and SENP2 play a critical role in

and nuclear pore complex function Kin-Hoe Chowa,*, Suzanne Elgorta, Mary Dassob, Maureen A. Powersc, and Katharine S. Ullmana aDepartment of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84112; bLaboratory of Gene Regulation and Development, National Institute for Child Health and Human Development,

Proteomic analysis of the mammalian nuclear pore complex

nuclear pore complex (NPC) has a vital cellular role. Nonetheless, much remains to be learned about many fundamental aspects of NPC function. To further understand the structure and function of the mammalian NPC, we have completed a proteomic analysis to identify and classify all of its protein components. We used mass

Structural basis for assembly and function of the Nup82

Nuclear pore complexes (NPCs), which are integrated into the double nuclear membrane, serve as the exclusive gateways to guide molecules between the nucleus and the cytoplasm.

DETERMINING FACTORS INFLUENCING NUCLEAR ENVELOPE AND NUCLEAR

cylindrical fissures called nuclear pores. These nuclear pores serve as sites for the assembly of one of the largest and most complex proteinaceous assemblies in the cell called the nuclear pore complexes (NPC), whose primary function is to facilitate transport of macromolecules between the nucleoplasm and the cytoplasm. The Nuclear pore complex.

Deep Insight Section

The nuclear pore complex: structure and function Duheron V, Fahrenkrog B Atlas Genet Cytogenet Oncol Haematol. 2015; 19(5) 357 translocation from the cytoplasmic filaments to the nuclear basket (Ben-Efraim and Gerace, 2001; Pyhtila and Rexach, 2003), it has now been shown that only FG-nucleoporins that are symmetrically

CELLULAR DYNAMICS Nongenetic functions of the genome

nuclear pore complex, and the DNA repair ma-chinery. The function of these cellular machin-eries is critically dependent on their binding tochromatin,butitisthephysicalpropertiesof RESEARCH SCIENCE sciencemag.org 6MAY2016 VOL 352 ISSUE 6286 aad6933-1 National Cancer Institute, Bethesda, MD 20892, USA.

The Role of Transcription Factors and Nuclear Pore Proteins

against a simple model for NPC function in transcriptional regu-lation. Thus, yeast TFs, together with nuclear pore proteins, play a critical role in controlling the spatial organization of the yeast genome. RESULTS AND DISCUSSION Gcn4 and Nup2 Play Direct Roles in Mediating Peripheral Gene Positioning

Pom121 links two essential subcomplexes of the nuclear pore

mation of the nuclear pore and the anchoring of the NPC to the pore membrane. Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane Jana M. Mitchell,1 Jörg Mansfeld, 2 Juliana Capitanio, 1 Ulrike Kutay, and Richard W. Wozniak 1Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7

Nuclear Pore Complex Function in Saccharomyces cerevisiae Is

Nuclear Pore Complex Function in Saccharomyces cerevisiae Is Influenced by Glycosylation of the Transmembrane Nucleoporin Pom152p Kenneth D. Belanger,*,1 Amitabha Gupta,*,2 Kristy M. MacDonald,* Christina M. Ott,*,3 Christine A. Hodge,† Charles M. Cole† and Laura I. Davis‡

Nuclear pore function viewed with atomic force microscopy

onstrating in fixed nuclear envelopes that, under condi-tions of depleted calcium stores of the nuclear cisternae, individual NPC appeared occluded whereas under store filling conditions they did not. ATP (in the presence of calcium) was necessary for refilling the stores [18] and for proper pore function [19]. Indeed, NPC is a dynamic

Functional analysis of Tpr: identification of nuclear pore

nuclear pore function. Through this analysis, we identi-fied an NH. 2-terminal domain that was sufficient for as-sociation with the nucleoplasmic aspect of the NPC. In addition, we unexpectedly found that the acidic COOH terminus was efficiently transported into the nuclear in-terior, an event that was apparently mediated by a pu-

Dissection of the NUP107 nuclear pore subcomplex reveals a

Mar 14, 2018 Nuclear pore complexes consist of several subcomplexes. The NUP107 complex is important for nucleocytoplasmic transport, nuclear envelope assembly and kinetochore function. However, the underlying molecular mechanisms and the roles of individual complex members remain elusive. We report the first description of a

Contribution of Electron Microscopy to the Study of the Nu

tion, immuno-gold electron microscopy has been used to reveal the molecular composition of the nuclear pore complex, and to dissect nuclear transport into distinct steps. This chapter reviews the contribution of several electron microscopy techniques to the study of the nuclear pore complex structure, composition and function.

Architecture of the fungal nuclear pore inner ring complex

The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the re constitution and interdisciplinary analyses of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar

The nuclear pore complex: a strategic platform for regulating

nuclear pore complex (NPC), nucleoporin. Summary Nuclear pore complexes (NPCs) are fundamental components of the eukaryotic cell. They perforate the nuclear envelope and serve as highly selective transport gates that enable bi-directional macromolecule exchange between the nucleus and cytoplasm. Recent studies

Quality control of mRNAs at the entry of the nuclear pore

[1,2]. mRNAs are exported through the nuclear pore complexes (NPCs), the nanochannels that perforate the nuclear envelope (NE) and primarily act as a gate-way for transport of various types of cargos (including mRNAs) into and out of the nucleus (see [3 8] for recent reviews on different aspects of NPC structure and function).

Functional association of Sun1 with nuclear pore complexes

the inner nuclear membranes (INMs) and outer nuclear membranes of mammalian nuclear envelopes. Both immunofl uorescence and immunoelectron microscopy re-veal that Sun1 but not Sun2 is intimately associated with nuclear pore complexes (NPCs). Topological analyses indicate that Sun1 is a type II integral protein of the INM.

Review Structure, dynamics and function of nuclear pore complexes

Structure, dynamics and function of nuclear pore complexes Maximiliano A. D Angelo and Martin W. Hetzer Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA Nuclearpore complexes are large aqueous channels that penetrate the nuclear envelope, thereby connecting the nuclear interior with the

Nuclear Pore Proteins in Regulation of Chromatin State

Nov 09, 2019 have low residence times at nuclear pores and to have intranuclear presence [15,16]. The existence of both on-pore and o -pore binding sites of Nups extends the functional reach of Nups in relation to chromatin structure, suggesting that the initially proposed connection between nuclear pores and

Nuclear Pore Composition and Gating in Herpes Simplex Virus

nuclear components, we examine some of the major nuclear pore constituents in infected versus uninfected cells and un-dertake a functional analysis of nuclear gating in live infected cells. We found no major perturbations in the total levels of major nucleoporins after infection or gross effects on sedimen-tation profiles in density gradients.

ClassicalNuclearLocalization Signals:Definition,Function

occurs through large, proteinaceous structures called nuclear pore complexes (NPCs) (6 9). Nuclear pore complexes allow passive diffusion of ions and small proteins (40 kDa) but restrict passage of larger molecules to those containing an appropriatetargetingsignal(10,11).Theporesareconstructed fromaclassofproteinscalled nucleoporins

THE NUCLEAR PORE

NUCLEAR PORE Nuclear pore complexes (NPCs) are huge molecular structures that penetrate the nucleus s two lipid bilayer membranes and mediate the transport of macromolecules into and out of the cell s command center. The structure of the NPC, which consists of more than 1,000 individual protein subunits, is coming into sharper focus, and

The nuclear pore complex structure and function at a glance

The nuclear pore complex structure and function at a glance Greg Kabachinski and Thomas U. Schwartz* ABSTRACT Nuclear pore complexes (NPCs) are indispensable for cell function and are at the center of several human diseases. NPCs provide access to the nucleus and regulate the transport of proteins and RNA across the nuclear envelope.

The Molecular Mechanism of Transport of Macromolecules

Nuclear Pore Complexes The trafficking of macromolecules, ions and small molecules between the nucleus and cytoplasm is mediated by nuclear pore complexes (NPCs), cylindrical proteina-ceous structures, about 1200 A ,in diameter and 700 A thick, that perforate the nuclear envelope (1,2). Vertebrate NPCs have an Mr of the order of 125000000 Da (3),

Roles of Nuclear Pores and Nucleo-Cytoplasmic Trafficking in

The nuclear pore complex (NPC) is a large protein complex that controls the exchange of components between the nucleus and the cytoplasm. In plants, the NPC family components play critical roles not only in essential growth and developmental processes, but also in plant responses to various environmental stress conditions.

Towards reconciling structure and function in the nuclear

the nucleus, the nuclear pore complex (NPC) has the princi-pal function of regulating the high throughput of nucleocy-toplasmic transport in a highly selective manner so as to maintain cellular order and function. Here, we present a ret-rospective review of the evidence that has led to the current understanding of both NPC structure and function.

The nuclear pore: at the crossroads

such as the nucleolus or the nuclear pore complex. This review will attempt to summarize some of the con-cepts that have emerged from studies carried out in many laboratories interested in nuclear transport. Primary among these advances is the realization that the nuclear pore com-plex has the potential for mediating the bidirectional trans-

Mutations in nuclear pore genes NUP93, NUP205, and XPO5 cause

Nucleoporins (NUPs) are highly conserved eukaryotic proteins that form nuclear pore complexes (NPCs), huge macromolecular assemblies in the nuclear envelope which mediate the transport of proteins, RNAs and RNP particles between cytoplasm and the nuclear interior (Supplementary Fig. 4). 25,17 NUPs function by interacting with transport receptors

The nuclear pore complex: bridging nuclear transport and gene

The nuclear pore complex: bridging nuclear transport and gene regulation Caterina Strambio-De-Castillia*‡, Mario Niepel§ and Michael P. Rout‡ Abstract Although the nuclear pore complex (NPC) is best known for its primary function as the key regulator of molecular traffic between the cytoplasm and the nucleus, a growing

The transport of integral membrane proteins across the

organizes the genome. The nuclear pore complexes embedded in the nuclear envelope allow selective transport of macromolecules between the cytosol and nucleoplasm, and as such help to control the flow of information from DNA to RNA to proteins. A growing list of inte-gral membrane proteins of the nuclear envelope are described to function in the

Glycosylation of the Nuclear Pore

of the role of glycosylation in nuclear pore function. Since that time, the O-GlcNAc field and the field of nucleocytoplasmic transport have developed in parallel. This review reports on the nexus between these fields. First, we outline the availability of new methods to label and isolate O-GlcNAc-modified proteins, as well

The nuclear pore complex: disease associations and functional

function is fulfilled by nuclear pore complexes (NPCs), which span the NE and provide a channel connecting the cytoplasm to the nucleus [1]. NPCs are very large structures with a mass of 60 125 MDa and a diameter of ,145 nm [3,61,62] (Figure I). Their most striking feature is their eightfold rotational symmetry, which is