Rab Gtpases
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Rab Gtpases
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Author : Guangpu Li (Molecular biologist)
language : en
Publisher:
Release Date : 2015
Rab Gtpases written by Guangpu Li (Molecular biologist) and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2015 with Biochemistry categories.
This volume covers the latest technological advances in the characterization of the biosynthesis and functions of Rab GTPases and their regulation by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs). The book consists of 28 chapters, and starts with an overview of the Rab GTPase family. The next few chapters describe systematic approaches to the identification and classification of Rabs and Rab GAPs, as well as the detection of Rab isoprenylation and membrane distribution. The last few chapters examine the biochemical and functional properties of individual Rabs in the order of exocytic, recycling, and endocytic Rabs. Written in the highly successful Methods of Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Instructive and practical, Rab GTPases: Methods and Protocols approaches each topic with great detail and is a valuable resource for researchers and students interested in the field of Rab GTPases.
Rab Gtpases And Membrane Trafficking
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Author : Guangpu Li
language : en
Publisher: Bentham Science Publishers
Release Date : 2012-05-21
Rab Gtpases And Membrane Trafficking written by Guangpu Li and has been published by Bentham Science Publishers this book supported file pdf, txt, epub, kindle and other format this book has been release on 2012-05-21 with Science categories.
"Ypt/Rab GTPases form the largest branch of the Ras-related small GTPase superfamily and regulate intracellular membrane trafficking in all eukaryotes. Since their discovery over two decades ago, a wealth of information has accumulated about the roles that"
Rab Gtpase Activating Proteins At The Golgi Endosome Interface
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Author : Ryan Michael Nottingham
language : en
Publisher: Stanford University
Release Date : 2010
Rab Gtpase Activating Proteins At The Golgi Endosome Interface written by Ryan Michael Nottingham and has been published by Stanford University this book supported file pdf, txt, epub, kindle and other format this book has been release on 2010 with categories.
Rab GTPases are master regulators of membrane trafficking in eukaryotic cells. With GTP bound, they regulate trafficking by recruiting effectors to specific membrane-bound compartments. GTPase-activating proteins (GAPs) stimulate a Rab's intrinsic rate of GTP hydrolysis, thus inactivating the Rab by converting bound GTP to GDP. Regulation of Rab proteins links the formation and breakdown of sequential, Rab-regulated membrane domains in the secretory and endocytic pathways. This thesis presents the characterization of a novel RabGAP, RUTBC1. RUTBC1 binds Rab9 in vitro and in cells through interactions with its N-terminus. Overexpression of RUTBC1 only slightly disrupts MPR trafficking and RUTBC1 does not function as a GAP for Rab9. In vitro biochemical screening of Rab proteins revealed that RUTBC1 has GAP activity toward Rab33b and Rab32. These data suggest that RUTBC1 might function to link inactivation of these Rabs in relation to a Rab9 microdomain, in support of the existence of a Rab cascade at the interface between the Golgi apparatus and endosomes. Depletion of RUTBC1 unexpectedly led to concomitant depletion of Atg16L1. Atg16L1 has an established and essential role in macroautophagy, a highly conserved cellular recycling process. Overexpression of Atg16L1 caused the formation of large puncta in the cytoplasm, which are also labeled by endogenous RUTBC1 and may represent autophagosomes. Atg16L1 is a known Rab33b effector, suggesting that Rab33b, RUTBC1 and Atg16L1 function together to regulate autophagosome formation. Finally, RUTBC2, which is highly related to RUTBC1, also binds specifically to Rab9. In vitro biochemical screening for RUTBC2's Rab substrates showed that RUTBC2 had highest GAP activity toward Rab34 and Rab36, two very similar Rabs thought to play a role in secretion. The difference in substrate specificity between RUTBC1 and RUTBC2 further exemplifies the highly complex integration of diverse membrane trafficking pathways in mammalian cells.
Gtpases Regulating Membrane Targeting And Fusion
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Author : W. E. Balch
language : en
Publisher: Gulf Professional Publishing
Release Date : 2005-12-13
Gtpases Regulating Membrane Targeting And Fusion written by W. E. Balch and has been published by Gulf Professional Publishing this book supported file pdf, txt, epub, kindle and other format this book has been release on 2005-12-13 with Science categories.
Rab GTPases now comprise a family of >63 members. They are emerging as the key hub element controlling the membrane architecture of eukaryotic cells. They are intimately involved in vesicle targeting and fusion in both the endocytic and exocytic pathways and direct the assembly and disassembly of protein complexes that include regulators (GEFs and GAPs), effectors (tethers/motors) and fusion components (SNAREs) that control membrane targeting and fusion. During the last 3 years the field has virtually exploded with the identification and characterization of many new Rab proteins and their effectors. Our understanding of how Rab GTPases control membrane function remains at its infancy. This volume of Methods in Enzymology, GTPases Regulating Membrane Targeting and Fusion, provides a wealth of new concepts, approaches and tools to study Rab proteins in the test tube and in living cells that will be of strong benefit to both established laboratories and new investigators in the field to elucidate Rab GTPase function in cellular development, differentiation and proliferation. Comprehensive overview of Rab GTPase phylogeny and systems biology Identification and characterization of Rab GEFs, GAPs and effectors General methodologies to study Rab GTPase function in vitro and in vivo using biochemical, molecular and microscopy approaches
Rab Gtpases And Their Binding Proteins In The Regulation Of Endocytic Events
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Author : Magdalena Deneka
language : en
Publisher:
Release Date : 2002
Rab Gtpases And Their Binding Proteins In The Regulation Of Endocytic Events written by Magdalena Deneka and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2002 with categories.
Membrane Binding Properties Of Rab Gtpases
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Author : Guillaume Kulakowski
language : en
Publisher:
Release Date : 2017
Membrane Binding Properties Of Rab Gtpases written by Guillaume Kulakowski and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2017 with categories.
RAB GTPases are major regulators of vesicular trafficking and localize to specific compartments. Deciphering the molecular mechanisms governing RAB localization is thus critical to understand intracellular transport processes. We have managed, for the first time, to incorporate purified and prenylated RABs into artificial membranes. By doing so, we observed that RAB6, but not RAB1 or RAB5, is able to promote by itself vesicle tethering. We believe that RAB6 is able to interact in trans with itself and to consequently drive homotypic membrane tethering. In the main part of this study, we investigated the physicochemical membrane requirements necessary for RAB recruitment. RAB1, RAB5 and RAB6 were all found to only localize to disordered membrane domains and to preferentially bind to curved membranes. We demonstrated that this specific recruitment of RAB1, RAB5 and RAB6 is primarily dependent on the hydrophobic insertion of their prenyl group into lipid packing defects. In contrast, RAB35 recruitment was primarily dependent on the presence of negatively charged lipids and was found to be modulated, to a lesser extent, by lipid packing defects. Although RAB4 and RAB11 were effectively recruited to purified Golgi fractions, in an effector-independent manner, membrane charges and lipid packing defects were not sufficient to promote their recruitment to synthetic vesicles; suggesting that RAB4 and RAB11 require more demanding membrane physicochemical properties. Our work demonstrates that the properties of membranes are critical for the regulation of RAB specific membrane targeting.
Regulators And Effectors Of Small Gtpases Rho Family
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Author :
language : en
Publisher: Elsevier
Release Date : 2006-02-21
Regulators And Effectors Of Small Gtpases Rho Family written by and has been published by Elsevier this book supported file pdf, txt, epub, kindle and other format this book has been release on 2006-02-21 with Science categories.
The Ras superfamily (>150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continually increasing, functionally complex array of downstream effectors. Since the last Methods in Enzymology volume on this topic in 2000, Rho GTPases have continued to receive a huge amount of attention. The human genome sequence has revealed the full extent of the Rho GEF and Rho GAP families (over 80 members for each) and the challenge of identifying the molecular interactions and cellular pathways influenced by each of these regulators is a daunting prospect. This new volume, Regulators and Effectors of Small GTPases: Rho Family, describes some of the methods currently being used to examine Rho family GTPase regulation at the biochemical and cellular level. Describes the methods currently being used to examine Rho family GTPase regulation at the biochemical and cellular levels Includes new imaging techniques that revolutionize the ability to visualize GTPase activities Over 150 international contributors
Rab Gtpase Activating Proteins At The Golgi Endosome Interface
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Author : Ryan Michael Nottingham
language : en
Publisher:
Release Date : 2010
Rab Gtpase Activating Proteins At The Golgi Endosome Interface written by Ryan Michael Nottingham and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2010 with categories.
Rab GTPases are master regulators of membrane trafficking in eukaryotic cells. With GTP bound, they regulate trafficking by recruiting effectors to specific membrane-bound compartments. GTPase-activating proteins (GAPs) stimulate a Rab's intrinsic rate of GTP hydrolysis, thus inactivating the Rab by converting bound GTP to GDP. Regulation of Rab proteins links the formation and breakdown of sequential, Rab-regulated membrane domains in the secretory and endocytic pathways. This thesis presents the characterization of a novel RabGAP, RUTBC1. RUTBC1 binds Rab9 in vitro and in cells through interactions with its N-terminus. Overexpression of RUTBC1 only slightly disrupts MPR trafficking and RUTBC1 does not function as a GAP for Rab9. In vitro biochemical screening of Rab proteins revealed that RUTBC1 has GAP activity toward Rab33b and Rab32. These data suggest that RUTBC1 might function to link inactivation of these Rabs in relation to a Rab9 microdomain, in support of the existence of a Rab cascade at the interface between the Golgi apparatus and endosomes. Depletion of RUTBC1 unexpectedly led to concomitant depletion of Atg16L1. Atg16L1 has an established and essential role in macroautophagy, a highly conserved cellular recycling process. Overexpression of Atg16L1 caused the formation of large puncta in the cytoplasm, which are also labeled by endogenous RUTBC1 and may represent autophagosomes. Atg16L1 is a known Rab33b effector, suggesting that Rab33b, RUTBC1 and Atg16L1 function together to regulate autophagosome formation. Finally, RUTBC2, which is highly related to RUTBC1, also binds specifically to Rab9. In vitro biochemical screening for RUTBC2's Rab substrates showed that RUTBC2 had highest GAP activity toward Rab34 and Rab36, two very similar Rabs thought to play a role in secretion. The difference in substrate specificity between RUTBC1 and RUTBC2 further exemplifies the highly complex integration of diverse membrane trafficking pathways in mammalian cells.
Studies On Membrane Association And Targeting Of Rab Gtpases
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Author : Anita Raquel Quintal Gomes
language : en
Publisher:
Release Date : 2002
Studies On Membrane Association And Targeting Of Rab Gtpases written by Anita Raquel Quintal Gomes and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2002 with categories.
Rab Gtpase Regulated Intracellular Trafficking And Activity Of G Protein Coupled Receptors
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Author : Jennifer Lynn Seachrist
language : en
Publisher:
Release Date : 2003
Rab Gtpase Regulated Intracellular Trafficking And Activity Of G Protein Coupled Receptors written by Jennifer Lynn Seachrist and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2003 with categories.