ArticleSmall GTPases2021
Identification of guanine nucleotide exchange factors that increase Cdc42 activity in primary human endothelial cells.
Article in Small GTPases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 27 citations in OpenAlex.
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- Endothelial tip-cell position, filopodia formation and biomechanics require BMPR2 expression and signaling.Communications biology · 2025Article
- The role of RAC1 in resistance to targeted therapies in cancer.Small GTPases · 2024Review
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- Cell-based optimization and characterization of genetically encoded location-based biosensors for Cdc42 or Rac activity.Journal of cell science · 2023Article
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- ARHGEF26 enhances Salmonella invasion and inflammation in cells and mice.PLoS pathogens · 2021Article
- Language Impairment with a Partial Duplication ofMolecular syndromology · 2020Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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