Ras-Specific GTPase-Activating Proteins-Structures, Mechanisms, and Interactions.

Cell Enlargement Down-Regulation / physiology Enzyme Activation / physiology GTP Phosphohydrolases / metabolism Gap Junctions / physiology Humans Molecular Structure Neurofibromin 1 / physiology ras GTPase-Activating Proteins / chemistry

Journal

Cold Spring Harbor perspectives in medicine
ISSN: 2157-1422
Titre abrégé: Cold Spring Harb Perspect Med
Pays: United States
ID NLM: 101571139

Informations de publication

Date de publication:
01 03 2019
Historique:
pubmed: 15 8 2018
medline: 7 7 2020
entrez: 15 8 2018
Statut: epublish

Résumé

Ras-specific GTPase-activating proteins (RasGAPs) down-regulate the biological activity of Ras proteins by accelerating their intrinsic rate of GTP hydrolysis, basically by a transition state stabilizing mechanism. Oncogenic Ras is commonly not sensitive to RasGAPs caused by interference of mutants with the electronic or steric requirements of the transition state, resulting in up-regulation of activated Ras in respective cells. RasGAPs are modular proteins containing a helical catalytic RasGAP module surrounded by smaller domains that are frequently involved in the subcellular localization or contributing to regulatory features of their host proteins. In this review, we summarize current knowledge about RasGAP structure, mechanism, regulation, and dual-substrate specificity and discuss in some detail neurofibromin, one of the most important negative Ras regulators in cellular growth control and neuronal function.

Identifiants

DOI: 10.1101/cshperspect.a031500 PMID: 30104198 PMC: PMC6396337
pubmed: 30104198
pii: cshperspect.a031500
doi: 10.1101/cshperspect.a031500
pmc: PMC6396337
pii:
doi:

Substances chimiques

Neurofibromin 1 0
ras GTPase-Activating Proteins 0
GTP Phosphohydrolases EC 3.6.1.-

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

Copyright © 2019 Cold Spring Harbor Laboratory Press; all rights reserved.

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Auteurs

Klaus Scheffzek (K)

Division of Biological Chemistry (Biocenter), Medical University of Innsbruck, A-6020 Innsbruck, Austria.

Giridhar Shivalingaiah (G)

Division of Biological Chemistry (Biocenter), Medical University of Innsbruck, A-6020 Innsbruck, Austria.

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Classifications MeSH

questionsmedicales.fr › Phénomènes physiologiques › Croissance et développement › Croissance › Processus de croissance cellulaire › Augmentation de la taille cellulaire › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Phénomènes physiologiques › Phénomènes pharmacologiques et toxicologiques › Phénomènes pharmacologiques › Régulation négative › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Métabolisme › Activation enzymatique › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Acid anhydride hydrolases › dGTPases › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › Structures de la membrane cellulaire › Jonctions intercellulaires › Jonctions communicantes › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Phénomènes chimiques › Structure moléculaire › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines tumorales › Protéines suppresseurs de tumeurs › Neurofibromine-1 › Ras-Specific GTPase-Activating...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Régulateurs des protéines G › Protéines d'activation de la GTPase › Protéines d'activation de la ras GTPase › Ras-Specific GTPase-Activating...