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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Knorre, Alexander Kolanus, Waldemar Famulok, Michael Theis, Mirko G. Kellersch, Bettina Moelleken, Jörg Wieland, Felix |
Description | Author Affiliation: Theis MG ( Kekulé Institut für Organische Chemie und Biochemie, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany.); |
Abstract | Cytohesins are a family of highly homologous guanine nucleotide exchange factors (GEFs) that act on ADP-ribosylation factors (ARFs). The small ARF-GEFs are involved in integrin signaling, actin cytoskeleton remodeling, and vesicle transport. Here, we selected and applied a specific inhibitor for ARF nucleotide-binding site opener (ARNO)/cytohesin-2, an RNA aptamer that clearly discriminates between cytohesin-1 and cytohesin-2. This reagent bound to an N-terminal segment of cytohesin-2 and did not inhibit ARF-GEF function in vitro. When transfected into HeLa cells, it persisted for at least 6 h without requiring stabilization. Its effect in vivo was to down-regulate gene expression mediated through the serum-response element and knockdown mitogen-activated protein kinase activation, indicating that cytohesin-2 acts by means of mitogen-activated protein kinase signaling. We conclude that the N-terminal coiled-coil and parts of the Sec7 domain of cytohesin-2 are required for serum-mediated transcriptional activation in nonimmune cells, whereas cytohesin-1 is not. Our results indicate that intramer technology can be used not only for assigning novel biological functions to proteins or protein domains but also to prove nonredundancy of highly homologous proteins. |
ISSN | 00278424 |
e-ISSN | 10916490 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Issue Number | 31 |
Volume Number | 101 |
Language | English |
Publisher | National Academy of Sciences |
Publisher Date | 2004-08-01 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | GTPase-Activating Proteins Genetics Metabolism Serum Response Element Transcriptional Activation Physiology ADP-Ribosylation Factors Cell Adhesion Molecules Chemistry Gene Expression Guanine Nucleotide Exchange Factors HeLa Cells MAP Kinase Signaling System Molecular Sequence Data Protein Structure, Tertiary RNA Transcription, Genetic Research Support, Non-U.S. Gov't Multidisciplinary |
Content Type | Text |
Resource Type | Article |
Subject | Multidisciplinary |
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