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Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells

The Rho GTPase family is involved in actin dynamics and regulates the barrier function of the endothelium. One of the main barrier-promoting Rho GTPases is Cdc42, also known as cell division control protein 42 homolog. Currently, regulation of Cdc42-based signalling networks in endothelial cells (EC...

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Autores principales: Reinhard, Nathalie R., Van Der Niet, Sanne, Chertkova, Anna, Postma, Marten, Hordijk, Peter L., Gadella Jr., Theodorus W.J., Goedhart, Joachim
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7939571/
https://www.ncbi.nlm.nih.gov/pubmed/31469028
http://dx.doi.org/10.1080/21541248.2019.1658509
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author Reinhard, Nathalie R.
Van Der Niet, Sanne
Chertkova, Anna
Postma, Marten
Hordijk, Peter L.
Gadella Jr., Theodorus W.J.
Goedhart, Joachim
author_facet Reinhard, Nathalie R.
Van Der Niet, Sanne
Chertkova, Anna
Postma, Marten
Hordijk, Peter L.
Gadella Jr., Theodorus W.J.
Goedhart, Joachim
author_sort Reinhard, Nathalie R.
collection PubMed
description The Rho GTPase family is involved in actin dynamics and regulates the barrier function of the endothelium. One of the main barrier-promoting Rho GTPases is Cdc42, also known as cell division control protein 42 homolog. Currently, regulation of Cdc42-based signalling networks in endothelial cells (ECs) lack molecular details. To examine these, we focused on a subset of 15 Rho guanine nucleotide exchange factors (GEFs), which are expressed in the endothelium. By performing single cell FRET measurements with Rho GTPase biosensors in primary human ECs, we monitored GEF efficiency towards Cdc42 and Rac1. A new, single cell-based analysis was developed and used to enable the quantitative comparison of cellular activities of the overexpressed full-length GEFs. Our data reveal GEF dependent activation of Cdc42, with the most efficient Cdc42 activation induced by PLEKHG2, FGD1, PLEKHG1 and PREX1 and the highest selectivity for FGD1. Additionally, we generated truncated GEF constructs that comprise only the catalytic dbl homology (DH) domain or together with the adjacent pleckstrin homology domain (DHPH). The DH domain by itself did not activate Cdc42, whereas the DHPH domain of ITSN1, ITSN2 and PLEKHG1 showed activity towards Cdc42. Together, our study characterized endothelial GEFs that may directly or indirectly activate Cdc42, which will be of great value for the field of vascular biology.
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spelling pubmed-79395712021-03-18 Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells Reinhard, Nathalie R. Van Der Niet, Sanne Chertkova, Anna Postma, Marten Hordijk, Peter L. Gadella Jr., Theodorus W.J. Goedhart, Joachim Small GTPases Research Paper The Rho GTPase family is involved in actin dynamics and regulates the barrier function of the endothelium. One of the main barrier-promoting Rho GTPases is Cdc42, also known as cell division control protein 42 homolog. Currently, regulation of Cdc42-based signalling networks in endothelial cells (ECs) lack molecular details. To examine these, we focused on a subset of 15 Rho guanine nucleotide exchange factors (GEFs), which are expressed in the endothelium. By performing single cell FRET measurements with Rho GTPase biosensors in primary human ECs, we monitored GEF efficiency towards Cdc42 and Rac1. A new, single cell-based analysis was developed and used to enable the quantitative comparison of cellular activities of the overexpressed full-length GEFs. Our data reveal GEF dependent activation of Cdc42, with the most efficient Cdc42 activation induced by PLEKHG2, FGD1, PLEKHG1 and PREX1 and the highest selectivity for FGD1. Additionally, we generated truncated GEF constructs that comprise only the catalytic dbl homology (DH) domain or together with the adjacent pleckstrin homology domain (DHPH). The DH domain by itself did not activate Cdc42, whereas the DHPH domain of ITSN1, ITSN2 and PLEKHG1 showed activity towards Cdc42. Together, our study characterized endothelial GEFs that may directly or indirectly activate Cdc42, which will be of great value for the field of vascular biology. Taylor & Francis 2019-08-30 /pmc/articles/PMC7939571/ /pubmed/31469028 http://dx.doi.org/10.1080/21541248.2019.1658509 Text en © 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Research Paper
Reinhard, Nathalie R.
Van Der Niet, Sanne
Chertkova, Anna
Postma, Marten
Hordijk, Peter L.
Gadella Jr., Theodorus W.J.
Goedhart, Joachim
Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title_full Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title_fullStr Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title_full_unstemmed Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title_short Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells
title_sort identification of guanine nucleotide exchange factors that increase cdc42 activity in primary human endothelial cells
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7939571/
https://www.ncbi.nlm.nih.gov/pubmed/31469028
http://dx.doi.org/10.1080/21541248.2019.1658509
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