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A Cytohesin Homolog in Dictyostelium Amoebae
BACKGROUND: Dictyostelium, an amoeboid motile cell, harbors several paralogous Sec7 genes that encode members of three distinct subfamilies of the Sec7 superfamily of Guanine nucleotide exchange factors. Among them are proteins of the GBF/BIG family present in all eukaryotes. The third subfamily rep...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826412/ https://www.ncbi.nlm.nih.gov/pubmed/20186335 http://dx.doi.org/10.1371/journal.pone.0009378 |
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author | Shina, Maria Christina Müller, Rolf Blau-Wasser, Rosemarie Glöckner, Gernot Schleicher, Michael Eichinger, Ludwig Noegel, Angelika A. Kolanus, Waldemar |
author_facet | Shina, Maria Christina Müller, Rolf Blau-Wasser, Rosemarie Glöckner, Gernot Schleicher, Michael Eichinger, Ludwig Noegel, Angelika A. Kolanus, Waldemar |
author_sort | Shina, Maria Christina |
collection | PubMed |
description | BACKGROUND: Dictyostelium, an amoeboid motile cell, harbors several paralogous Sec7 genes that encode members of three distinct subfamilies of the Sec7 superfamily of Guanine nucleotide exchange factors. Among them are proteins of the GBF/BIG family present in all eukaryotes. The third subfamily represented with three members in D. discoideum is the cytohesin family that has been thought to be metazoan specific. Cytohesins are characterized by a Sec7 PH tandem domain and have roles in cell adhesion and migration. PRINCIPAL FINDINGS: Dictyostelium SecG exhibits highest homologies to the cytohesins. It harbors at its amino terminus several ankyrin repeats that are followed by the Sec7 PH tandem domain. Mutants lacking SecG show reduced cell-substratum adhesion whereas cell-cell adhesion that is important for development is not affected. Accordingly, multicellular development proceeds normally in the mutant. During chemotaxis secG(−) cells elongate and migrate in a directed fashion towards cAMP, however speed is moderately reduced. SIGNIFICANCE: The data indicate that SecG is a relevant factor for cell-substrate adhesion and reveal the basic function of a cytohesin in a lower eukaryote. |
format | Text |
id | pubmed-2826412 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-28264122010-02-26 A Cytohesin Homolog in Dictyostelium Amoebae Shina, Maria Christina Müller, Rolf Blau-Wasser, Rosemarie Glöckner, Gernot Schleicher, Michael Eichinger, Ludwig Noegel, Angelika A. Kolanus, Waldemar PLoS One Research Article BACKGROUND: Dictyostelium, an amoeboid motile cell, harbors several paralogous Sec7 genes that encode members of three distinct subfamilies of the Sec7 superfamily of Guanine nucleotide exchange factors. Among them are proteins of the GBF/BIG family present in all eukaryotes. The third subfamily represented with three members in D. discoideum is the cytohesin family that has been thought to be metazoan specific. Cytohesins are characterized by a Sec7 PH tandem domain and have roles in cell adhesion and migration. PRINCIPAL FINDINGS: Dictyostelium SecG exhibits highest homologies to the cytohesins. It harbors at its amino terminus several ankyrin repeats that are followed by the Sec7 PH tandem domain. Mutants lacking SecG show reduced cell-substratum adhesion whereas cell-cell adhesion that is important for development is not affected. Accordingly, multicellular development proceeds normally in the mutant. During chemotaxis secG(−) cells elongate and migrate in a directed fashion towards cAMP, however speed is moderately reduced. SIGNIFICANCE: The data indicate that SecG is a relevant factor for cell-substrate adhesion and reveal the basic function of a cytohesin in a lower eukaryote. Public Library of Science 2010-02-23 /pmc/articles/PMC2826412/ /pubmed/20186335 http://dx.doi.org/10.1371/journal.pone.0009378 Text en Shina et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Shina, Maria Christina Müller, Rolf Blau-Wasser, Rosemarie Glöckner, Gernot Schleicher, Michael Eichinger, Ludwig Noegel, Angelika A. Kolanus, Waldemar A Cytohesin Homolog in Dictyostelium Amoebae |
title | A Cytohesin Homolog in Dictyostelium Amoebae |
title_full | A Cytohesin Homolog in Dictyostelium Amoebae |
title_fullStr | A Cytohesin Homolog in Dictyostelium Amoebae |
title_full_unstemmed | A Cytohesin Homolog in Dictyostelium Amoebae |
title_short | A Cytohesin Homolog in Dictyostelium Amoebae |
title_sort | cytohesin homolog in dictyostelium amoebae |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826412/ https://www.ncbi.nlm.nih.gov/pubmed/20186335 http://dx.doi.org/10.1371/journal.pone.0009378 |
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