Last edited by Mara
Wednesday, August 12, 2020 | History

6 edition of The Small GTPase Ran found in the catalog.

The Small GTPase Ran

  • 199 Want to read
  • 15 Currently reading

Published by Springer .
Written in English

    Subjects:
  • Proteins,
  • Oncology,
  • Science,
  • Computer Books: General,
  • Immunology,
  • Life Sciences - Biochemistry,
  • Medical : Immunology,
  • Medical : Oncology,
  • Science / Biochemistry,
  • G proteins,
  • Guanosine triphosphatase

  • Edition Notes

    ContributionsMark Rush (Editor), Peter D"Eustachio (Editor)
    The Physical Object
    FormatHardcover
    Number of Pages214
    ID Numbers
    Open LibraryOL9676406M
    ISBN 100792375106
    ISBN 109780792375104

    (GDIs bind to small Rho and Rab GDP-bound GTPases and keep the GTPase inactivated, as well as preventing the GTPase from localizing at their place of action, their membrane.) GTP analogues that cannot be hydrolyzed (γ-S-GTP, β,γ-methylene-GTP, and β,γ-imino-GTP) can keep GTPase active. Ran is a small ras-related GTPase that controls the nucleocytoplasmic exchange of macromolecules across the nuclear envelope. It binds to chromatin early during nuclear formation and has important roles during the eukaryotic cell cycle, where it regulates mitotic spindle assembly, nuclear envelope formation and cell cycle checkpoint control.

    Small GTPases are a large family of hydrolases that bind and hydrolyze GTP to GDP in order to regulate many cellular activities (e.g., cell differentiation, proliferation, and motility) [].Inherently, small GTPases have a basal mild endogenous GTPase activity that is dependent on Mg 2+ to weaken the bond between the last two phosphates in GTP in order to form GDP [2,3,4].Cited by: 5. Most of the small GTPase superfamily members can be classified into 5 distinct subfamilies: Ras, Rho/Rac, Rab, Arf/Sar1 and Ran. Members within each subfamily share of the order of 40% or more amino acid sequence identity and exhibit conserved motifs required for interaction with specific classes of downstream effectors.

    ARF GTPase-Activating Protein 1 Irit Huber, Edna Cukierman, Miriam Rotman, and Dan Cassel Ran GTPases The Use of Permeabilized Cell Systems to Study Nuclear Transport Amy M. Brownawell, James M. Holaska, Ian G. Macara, and Bryce M. Paschal Analysis of Nuclear Protein Import and Export In Vitro Using Fluorescent CargoesPrice: $   Sar1, one of the five core COPII components, is a highly conserved small GTPase, which, upon GTP binding, recruits the other COPII proteins to the ER membrane. It has been hypothesized that the changes in the kinetics of SAR1 GTPase may .


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The Small GTPase Ran Download PDF EPUB FB2

The Small GTPase The Small GTPase Ran book Medicine & Health Science Books @ Skip to main content. Try Prime EN Hello, Sign in Account & Lists Sign in Account & Lists Returns & Orders Try Prime Cart. Books. Go Search Hello Select your address 5/5(1).

Open Library is an open, editable library catalog, building towards a web page for every book ever published. The Small Gtpase Ran by Mark Rush,Springer edition, paperback The Small Gtpase Ran ( edition) | Open Library. The Ras-related nuclear protein Ran is a member of the so-called Ras-superfamily of small GTP-binding proteins and hydrolyzing proteins.

This book aims to provide specialists with a summary of some of the research in this area, along with background describing its initial identification and early characterization.

The Small GTPase Ran. Editors: Rush, Mark, D'Eustachio, Peter (Eds.) Free Preview. Buy this book eB29 € price for Spain (gross) Buy eBook ISBN ; Digitally watermarked, DRM-free; Included format: PDF, EPUB; ebooks can be. The Small GTPase Ran. Editors (view affiliations) Mark Rush; Peter D’Eustachio; Search within book.

Front Matter. Pages i-xxiii. PDF. The Role of Ran in Nuclear Import Ran GTPASE Regulation of the CRM1-Dependent Export Pathway. Bryce M. Paschal, Catherine Dargemont. Pages Role of Ran GTPase in RNA Processing and Export of. Find helpful customer reviews and review ratings for The Small GTPase Ran at Read honest and unbiased product reviews from our users a stimulating and interesting anthology that covers the first decade of Ran research" "As a whole the book also serves as an excellent reference source because virtually all available data on Ran 5/5(1).

The Small GTPase Ran is meant to provide specialists with a concise summary of some of the recent research in this area, along with background describing its initial identification and early characterization.\/span>\"@ en\/a> ; \u00A0\u00A0\u00A0\n schema:description\/a> \" 1.

The Role of Ran in Nuclear Import -- 1. Canonical mutations that affect the GTPase cycle lead to constitutively-active or dominant-negative molecules (Bourne et al., ).Mutations that abolish GTPase activity (e.g., glycine 12 to valine; G12V) result in constitutive activation of the small GTPase, and mutations that presumably affect interaction of the GTPase with its effectors (e.g., threonine 17 to.

Elliott M. Ross, in Methods in Enzymology, Steady-State GTPase Assays. GTPase assays are carried out at 30° in a total volume of 30–50 μl in polypropylene tubes for 15 min or less, according to the total GTPase activity and the needs of the experiment.

It is generally convenient to prepare a cocktail of assay reagents and to add to it the vesicles, GAP, and any other. To classify Arabidopsis small GTPase genes into Ras, Rho, Rab, Arf, and Ran families, theoretical protein sequences from these genes were aligned to previously compiled lists of small GTPases of S.

cerevisiae and humans using ClustalW (Thompson et al., ) and then edited manually to restrict phylogenetic analysis to conserved “core. An ironic feature of small GTPases, which frequently confuses newcomers, is that the enzymatic function of small GTPases—GTP hydrolysis to generate GDP and free inorganic phosphate—inactivates the protein.

Thus selectively altering the catalytic function of a small GTPase without disrupting protein structure locks the protein inFile Size: 2MB. The Small GTPase Ran Edited by: the progress of research on Ran illustrated in this book has been advanced by a variety of different model organisms.

The Small GTPase Ran. The book cover shows the structure of Ran in ribbon representation, highlighting the conformational differences between its GTP (blue) and GDP bound (green) forms, respectively.

(By K. Scheffzek; see page ) The Small GTPase Ran edited by. Previous studies indicated that GTPase activity is required for vesicle fusion (Boman et al., ; Ulitzur et al., ).

Ran is a small GTPase that plays a role in nuclear export and import and in mitotic spindle formation (Macara, ; Moore, ).

During mitosis, Ran is also associated with mitotic chromosomes and it appears to play a. Small GTPases of the Ras superfamily are key regulators of diverse cellular and developmental events, including differentiation, cell division, vesicle transport, nuclear assembly, and control of the cytoskeleton.

The C. elegans genome encodes 56 members of the major Ras GTPase subfamilies, including the Ras/Ral/Rap family, the Rho family, the Rab family, Ran, Author: Erik A.

Lundquist. Small GTPases typically function as nodal points that integrate broad upstream regulatory inputs and disseminate broad effector outputs.

The superfamily comprises five families that are conserved across eukaryotes: Ras, Rho, Rab, Arf, and Ran. Abstract. Like many other small GTPases, Ran functions in eukaryotic cells as a molecular switch that cycles between GTP- and GDP-bound forms.

Through the proper modulation of the GTP/GDP cycle, Ran functions with a number of Ran-binding proteins to control a broad array of fundamental cellular functions, including nucleocytoplasmic transport, mitotic Cited by: 9.

Small GTPase binding proteins (GTPases) are an ancient group of proteins that play key roles in almost every aspect of cell biology, from cell proliferation to nuclear transport. In GTPase Protocols: The Ras Superfamily, Edward J.

Manser and Thomas Leung have collected the key techniques currently in use to probe the function of these. The Small GTPase Ran The Ras-related nuclear protein Ran is a member of the so-called Ras-superfamily of small GTP-binding proteins and hydrolyzing proteins.

A variety of edited anthologies related to the Ras-superfamily have appeared over the last decade, but Ran has been under-represented in Brand: Ed Dasso. Most Small GTPases Are Highly Conserved Regulators of Intracellular Trafficking.

The small GTPase superfamily is divided into at least five families, including Ras, Rho, Rab, Arf, and Ran (Bischoff et al., ; Takai et al., ).The Rab, Arf, and Ran families are conserved in eukaryotes and directly participate in the regulation of eukaryotic hallmark cellular processes. The driving force behind nuclear import is provided by the predominant nuclear localization of a small GTPase, called Ran (Gsp1), in its GTP-bound state,40 The gradient of RanGTP across the NPC is established by the exclusive nuclear or cytoplasmic localization of its guanine-exchange factor (Ran-GEF) and its GTPase activating protein (Ran-GAP), respectively.One essential regulator of this process is Ran-specific GTPase-activating protein (RanBP 1), which also catalyzes the GTP hydrolysis of Ran.

It has .Interaction between the small GTPase Ran/Gsp1p and Ntf2p is required for nuclear transport Article (PDF Available) in Molecular and Cellular Biology 17(7) .