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Author: Jeffrey Hsin Nien Tang Publisher: ISBN: Category : Languages : en Pages : 103
Book Description
The nuclear pore complex (NPC) is one of the largest known protein structures in the cell. Evolutionarily conserved in eukaryotes ranging from fungi to plants and animals, the NPC is the main transporter of molecules between the cell cytoplasm and nucleus. Maintaining the proper compartment-specific localization of proteins and RNA is crucial for normal cell function, and the nuclear pore accomplishes this task both robustly and efficiently. Over the past several decades, insight into the composition, organization, structure, and mechanism of the NPC has been gradually teased out through careful experimentation. However, many questions about the pore's function remain unanswered. In this dissertation, I describe efforts aimed at elucidating several aspects of the NPC. First, I investigate the transport properties of the pore, specifically looking at how the nuclear transport receptor importin-[beta] and the Ran GTPase interact not only with each other but also how they may affect the pore itself. The nucleoporin Nup153 is identified as an important player in the nuclear transport process which binds strongly to importin-[beta] in a Ran-sensitive manner. Using multiple experimental techniques, the properties of importin-[beta], and Nup153's interactions are characterized and shown to be capable of modulating the selective permeability barrier of the NPC. Next, I examine how members of a major class of nuclear pore proteins, the scaffold nucleoporins, are both structurally and functionally similar to the karyopherin family of soluble nuclear transport receptors. Structures of the proteins Nup188 and Nup192 are analyzed and shown to resemble those of karyopherins. Furthermore, in vitro assays indicate that at least a subset of the scaffold nucleoporins behave functionally as transport receptors, hinting at an evolutionary relationship between these two important classes of proteins. Finally, a calcium-mediated phenomenon affecting the permeability of the NPC is explored. I show that certain cytosolic proteases are activated by millimolar concentrations of calcium ion which leads irreversibly to an increase in the nuclear pore's permeability to large molecules. A model for physiological pathways implicated in this effect is proposed.
Author: Jeffrey Hsin Nien Tang Publisher: ISBN: Category : Languages : en Pages : 103
Book Description
The nuclear pore complex (NPC) is one of the largest known protein structures in the cell. Evolutionarily conserved in eukaryotes ranging from fungi to plants and animals, the NPC is the main transporter of molecules between the cell cytoplasm and nucleus. Maintaining the proper compartment-specific localization of proteins and RNA is crucial for normal cell function, and the nuclear pore accomplishes this task both robustly and efficiently. Over the past several decades, insight into the composition, organization, structure, and mechanism of the NPC has been gradually teased out through careful experimentation. However, many questions about the pore's function remain unanswered. In this dissertation, I describe efforts aimed at elucidating several aspects of the NPC. First, I investigate the transport properties of the pore, specifically looking at how the nuclear transport receptor importin-[beta] and the Ran GTPase interact not only with each other but also how they may affect the pore itself. The nucleoporin Nup153 is identified as an important player in the nuclear transport process which binds strongly to importin-[beta] in a Ran-sensitive manner. Using multiple experimental techniques, the properties of importin-[beta], and Nup153's interactions are characterized and shown to be capable of modulating the selective permeability barrier of the NPC. Next, I examine how members of a major class of nuclear pore proteins, the scaffold nucleoporins, are both structurally and functionally similar to the karyopherin family of soluble nuclear transport receptors. Structures of the proteins Nup188 and Nup192 are analyzed and shown to resemble those of karyopherins. Furthermore, in vitro assays indicate that at least a subset of the scaffold nucleoporins behave functionally as transport receptors, hinting at an evolutionary relationship between these two important classes of proteins. Finally, a calcium-mediated phenomenon affecting the permeability of the NPC is explored. I show that certain cytosolic proteases are activated by millimolar concentrations of calcium ion which leads irreversibly to an increase in the nuclear pore's permeability to large molecules. A model for physiological pathways implicated in this effect is proposed.
Author: Karsten Weis Publisher: Springer Science & Business Media ISBN: 3540446036 Category : Science Languages : en Pages : 222
Book Description
Bidirectional traffic of macromolecules across the nuclear envelope is an active and essential transport process in all eukaryotic cells. Work on various model systems has led to a tremendous increase in our understanding of nuclear transport in recent years. This volume summarizes our current knowledge of protein and RNA transport into and out of the nucleus. It contains nine up-to-date reviews which cover various aspects of nucleocytoplasmic transport, including the structure and function of the nuclear pore complex, the role of soluble transport factors in protein and RNA transport, and the regulation of protein transport through the nuclear pore.
Author: Weidong Yang Publisher: Springer ISBN: 3319773097 Category : Science Languages : en Pages : 274
Book Description
Dysfunction of nuclear-cytoplasmic transport systems has been associated with many human diseases. Thus, understanding of how functional this transport system maintains, or through dysfunction fails to maintain remains the core question in cell biology. In eukaryotic cells, the nuclear envelope (NE) separates the genetic transcription in the nucleus from the translational machinery in the cytoplasm. Thousands of nuclear pore complexes (NPCs) embedded on the NE selectively mediate the bidirectional trafficking of macromolecules such as RNAs and proteins between these two cellular compartments. In this book, the authors integrate recent progress on the structure of NPC and the mechanism of nuclear-cytoplasmic transport system in vitro and in vivo.
Author: Publisher: Elsevier ISBN: 0124171788 Category : Science Languages : en Pages : 553
Book Description
Volume 122 of Methods in Cell Biology describes modern tools and techniques used to study nuclear pore complexes and nucleocytoplasmic transport in diverse eukaryotic model systems (including mammalian cells, Xenopus, C. elegans, yeast). The volume enables investigators to analyze nuclear pore complex structure, assembly, and dynamics; to evaluate protein and RNA trafficking through the nuclear envelope; and to design in vivo or in vitro assays appropriate to their research needs. Beyond the study of nuclear pores and transport as such, these protocols will also be helpful to scientists characterizing gene regulation, signal transduction, cell cycle, viral infections, or aging. The NPC being one of the largest multiprotein complexes in the cell, some protocols will also be of interest for people currently characterizing other macromolecular assemblies. This book is thus designed for laboratory use by graduate students, technicians, and researchers in many molecular and cellular disciplines. Describes modern tools and techniques used to study nuclear pore complexes and nucleocytoplasmic transport in diverse eukaryotic model systems (mammalian cells, Xenopus, C. elegans, yeast) Chapters are written by experts in the field Cutting-edge material
Author: Ambikanandan Misra Publisher: Elsevier ISBN: 0123849659 Category : Science Languages : en Pages : 686
Book Description
Delivery of therapeutic proteomics and genomics represent an important area of drug delivery research. Genomics and proteomics approaches could be used to direct drug development processes by unearthing pathways involved in disease pathogenesis where intervention may be most successful. This book describes the basics of genomics and proteomics and highlights the various chemical, physical and biological approaches to protein and gene delivery. Covers a diverse array of topics from basic sciences to therapeutic applications of proteomics and genomics delivery Of interest to researchers in both academia and industry Highlights what’s currently known and where further research is needed
Author: Mohammad Azimi Publisher: ISBN: Category : Languages : en Pages : 166
Book Description
Selective yet efficient transport between the cell nucleus and cytoplasm is critical to cellular function as the nuclear pore complex is a major point of regulation for gene expression, signal transduction, immune response, oncogenesis and viral propagation. The combined physical structure of the pore, biochemical interaction of transport factors with pore components and the presence of the cellular milieu create conditions under which selective and efficient nucleocytoplasmic transport can occur. In this dissertation, I explore the significance of structure and interaction on transport of globular proteins and polymeric mRNA cargo through the crowded pore. In the first part of this work, an agent based modeling software framework is developed and validated for accurately simulating discrete and stochastic reaction-diffusion systems. A simulation environment representing the structure of the nuclear pore complex along with rules for the dynamics of protein movement and interaction was created using in vivo and in vitro reported parameters. This setup was then used to perform in silico experiments on the role of pore-cargo affinity in optimizing transport efficiency. These experiments demonstrate the pore's sensitivity to cargo affinity in maintaining efficient transport and suggest that a higher affinity binding site at the side of the pore where transport is terminated increases efficiency by reducing futile shuttling of cargo complexes. In the final part of this dissertation, I extend my agent based modeling framework to look at aspects of mRNA export that have remained unaddressed in experimental works. Variations in the number and spacing of transport receptors bound to the mRNA are shown to play a critical role in transport efficiency. In these experiments, a single transport receptor at the 5' end appeared insufficient for facilitating export. Increasing transport receptor coverage along the length of the mRNA improved the chances of successful export. Additionally, it was observed that the presence of a transport receptor near either the 5' or 3' terminus is required for successful export as it likely promotes the emergence of a favorable threading conformation. Finally, it was observed that the use of a single fluorescent tag to track and report mRNA export time, as is standard in current experimental work, is likely to underestimate true transport times. These findings have implications in the design of targeted delivery and export of polymeric molecules into and out the nucleus.
Author: Paul S. Agutter Publisher: Springer Science & Business Media ISBN: 3662225026 Category : Science Languages : en Pages : 205
Book Description
The means by which proteins and RNAs are exchanged between cytoplasm and nucleus have interested cell biologists for many years, and the field has seen a number of exciting recent advances. Much has been learned about the intricate architecture of the nuclear pore-complex, the mechanisms by which transport substrates are sorted, and the supply of energy for exchange processes. This book attempts a general review of the growing body of knowledge. However, the authors challenge the presumptions implicit in some interpretations of the evidence, re-examining the concept of "transport" within cells, and suggesting that lessons learned from nucleocytoplasmic transport studies can elucidate wider aspects of cell biology.
Author: Paul S. Agutter Publisher: Springer ISBN: 9783540613510 Category : Science Languages : en Pages : 200
Book Description
The means by which proteins and RNAs are exchanged between cytoplasm and nucleus have interested cell biologists for many years, and the field has seen a number of exciting recent advances. Much has been learned about the intricate architecture of the nuclear pore-complex, the mechanisms by which transport substrates are sorted, and the supply of energy for exchange processes. This book attempts a general review of the growing body of knowledge. However, the authors challenge the presumptions implicit in some interpretations of the evidence, re-examining the concept of "transport" within cells, and suggesting that lessons learned from nucleocytoplasmic transport studies can elucidate wider aspects of cell biology.
Author: Jeffrey Hsin Nien Tang
Author: Jeffrey Hsin Nien Tang
Author: Karsten Weis
Author: Reiner Peters
Author: Weidong Yang
Author: 
Author: Ambikanandan Misra
Author: Karsten Weis
Author: Mohammad Azimi
Author: Paul S. Agutter
Author: Paul S. Agutter