NDLI: Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers.

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Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mayer, G. Böhm, T. Blind, M. Famulok, M. Kolanus, W. Jackson, C. L. Nagel, W. Knorr, T.
Description	Author Affiliation: Mayer G ( Kekulé-Institut für Organische Chemie und Biochemie, Rheinische Friedrich-Wilhelms Universität Bonn, Gerhard-Domagk Strasse 1, D-53121 Bonn, Germany.);
Abstract	ADP-ribosylation factor (ARF) GTPases and their regulatory proteins have been implicated in the control of diverse biological functions. Two main classes of positive regulatory elements for ARF have been discovered so far: the large Sec7/Gea and the small cytohesin/ARNO families, respectively. These proteins harbor guanine-nucleotide-exchange factor (GEF) activity exerted by the common Sec7 domain. The availability of a specific inhibitor, the fungal metabolite brefeldin A, has enabled documentation of the involvement of the large GEFs in vesicle transport. However, because of the lack of such tools, the biological roles of the small GEFs have remained controversial. Here, we have selected a series of RNA aptamers that specifically recognize the Sec7 domain of cytohesin 1. Some aptamers inhibit guanine-nucleotide exchange on ARF1, thereby preventing ARF activation in vitro. Among them, aptamer M69 exhibited unexpected specificity for the small GEFs, because it does not interact with or inhibit the GEF activity of the related Gea2-Sec7 domain, a member of the class of large GEFs. The inhibitory effect demonstrated in vitro clearly is observed as well in vivo, based on the finding that M69 produces similar results as a dominant-negative, GEF-deficient mutant of cytohesin 1: when expressed in the cytoplasm of T-cells, M69 reduces stimulated adhesion to intercellular adhesion molecule-1 and results in a dramatic reorganization of F-actin distribution. These highly specific cellular effects suggest that the ARF-GEF activity of cytohesin 1 plays an important role in cytoskeletal remodeling events of lymphoid cells.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Guanine Nucleotide Exchange Factors Antagonists & Inhibitors Metabolism RNA Pharmacology Saccharomyces Cerevisiae Proteins ADP-Ribosylation Factor 1 Actins Amino Acid Sequence Cell Adhesion Drug Effects Cell Adhesion Molecules Chemistry Genetics Cell Size Cytoskeleton Fungal Proteins Guanosine Diphosphate Guanosine Triphosphate Intercellular Adhesion Molecule-1 Jurkat Cells Molecular Sequence Data Mutation Nucleic Acid Conformation Protein Binding Protein Structure, Tertiary Substrate Specificity T-Lymphocytes Cytology Tetradecanoylphorbol Acetate Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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