Nucleophosmin1 is a negative regulator of the small GTPase Rac1
Autor: | Peter L. Hordijk, Paula B. van Hennik, Anne M. van Stalborgh, Younes Zoughlami |
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Přispěvatelé: | Landsteiner Laboratory, Physiology |
Jazyk: | angličtina |
Rok vydání: | 2013 |
Předmět: |
rac1 GTP-Binding Protein
Cytoplasm Cell division Signaling in cellular processes Regulator lcsh:Medicine Biology Signal transduction Signaling Pathways Cell Line Molecular cell biology Cell Adhesion Humans Small GTPase Cytoskeleton Nucleoplasmins lcsh:Science GTPase signaling Cell Nucleus Multidisciplinary Microscopy Confocal Cell Death Effector Mechanisms of Signal Transduction lcsh:R Subcellular localization Cellular Structures Cell biology Nuclear signaling Membrane protein Microscopy Fluorescence Cell movement signaling lcsh:Q Nucleophosmin Cell Division HeLa Cells Research Article |
Zdroj: | PLoS ONE, Vol 8, Iss 7, p e68477 (2013) PLoS ONE PLoS ONE, 8(7). Public Library of Science Zoughlami, Y, van Stalborgh, A M, van Hennik, P B & Hordijk, P L 2013, ' Nucleophosmin1 Is a Negative Regulator of the Small GTPase Rac1 ', PLoS ONE, vol. 8, no. 7, e68477 . https://doi.org/10.1371/journal.pone.0068477 PLoS ONE, 8(7):e68477. Public Library of Science |
ISSN: | 1932-6203 |
DOI: | 10.1371/journal.pone.0068477 |
Popis: | The Rac1 GTPase is a critical regulator of cytoskeletal dynamics and controls many biological processes, such as cell migration, cell-cell contacts, cellular growth and cell division. These complex processes are controlled by Rac1 signaling through effector proteins. We have previously identified several effector proteins of Rac1 that also act as Rac1 regulatory proteins, including caveolin-1 and PACSIN2. Here, we report that Rac1 interacts through its C-terminus with nucleophosmin1 (NPM1), a multifunctional nucleo-cytoplasmic shuttling protein with oncogenic properties. We show that Rac1 controls NPM1 subcellular localization. In cells expressing active Rac1, NPM1 translocates from the nucleus to the cytoplasm. In addition, Rac1 regulates the localization of the phosphorylated pool of NPM1 as this pool translocated from the nucleus to the cytosol in cells expressing activated Rac1. Conversely, we found that expression of NPM1 limits Rac1 GTP loading and cell spreading. In conclusion, this study identifies NPM1 as a novel, negative regulator of Rac1. |
Databáze: | OpenAIRE |
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