Cargando…
The N-Terminal DH-PH Domain of Trio Induces Cell Spreading and Migration by Regulating Lamellipodia Dynamics in a Rac1-Dependent Fashion
The guanine-nucleotide exchange factor Trio encodes two DH-PH domains that catalyze nucleotide exchange on Rac1, RhoG and RhoA. The N-terminal DH-PH domain is known to activate Rac1 and RhoG, whereas the C-terminal DH-PH domain can activate RhoA. The current study shows that the N-terminal DH-PH dom...
Autores principales: | van Rijssel, Jos, Hoogenboezem, Mark, Wester, Lynn, Hordijk, Peter L., Van Buul, Jaap D. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3253119/ https://www.ncbi.nlm.nih.gov/pubmed/22238672 http://dx.doi.org/10.1371/journal.pone.0029912 |
Ejemplares similares
-
The many faces of the guanine-nucleotide exchange factor trio
por: van Rijssel, Jos, et al.
Publicado: (2012) -
The Rho-guanine nucleotide exchange factor Trio controls leukocyte transendothelial migration by promoting docking structure formation
por: van Rijssel, Jos, et al.
Publicado: (2012) -
Flow-induced endothelial cell alignment requires the RhoGEF Trio as a scaffold protein to polarize active Rac1 distribution
por: Kroon, Jeffrey, et al.
Publicado: (2017) -
The RhoGEF Trio: A Protein with a Wide Range of Functions in the Vascular Endothelium
por: Kempers, Lanette, et al.
Publicado: (2021) -
The Rho-GEF Trio regulates a novel pro-inflammatory pathway through the transcription factor Ets2
por: Van Rijssel, Jos, et al.
Publicado: (2013)