Formation of complexes involving RasGAP and p190 RhoGAP during morphogenetic events of the gastrulation in Xenopus
Autor: | Marie Blancq, Henri Dupont |
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Rok vydání: | 1999 |
Předmět: |
Xenopus
Fluorescent Antibody Technique p38 Mitogen-Activated Protein Kinases Biochemistry Animals Guanine Nucleotide Exchange Factors Phosphorylation Cytoskeleton Adaptor Proteins Signal Transducing GRB2 Adaptor Protein biology Kinase Gene Expression Regulation Developmental Nuclear Proteins Proteins Signal transducing adaptor protein Gastrula Phosphoproteins biology.organism_classification Cell biology Gastrulation Adaptor Proteins Vesicular Transport Shc Signaling Adaptor Proteins ras GTPase-Activating Proteins biology.protein GRB2 Guanine nucleotide exchange factor Mitogen-Activated Protein Kinases Signal transduction Protein Binding Signal Transduction |
Zdroj: | European Journal of Biochemistry. 265:530-538 |
ISSN: | 1432-1033 0014-2956 |
Popis: | In relation to the activation of the Src-family of tyrosine kinases during early morphogenetic events of gastrulation in Xenopus, we have identified two multiprotein complexes. The first complex, including RasGAP, p190 RhoGAP and p62, was previously characterized in murine fibroblasts overexpressing c-Src or transformed by v-Src and has been correlated with cytoskeleton remodelling. A second complex, not identified in other models includes tyrosine-phosphorylated p66SHC, Grb2, RasGAP and p190 RhoGAP. The association with p66SHC, considered as a negative regulator of ERK (extracellular signal-regulated kinase), p120RasGAP and p190RhoGAP, suggests a possible mechanism for coupling Ras and Rho signalling pathways. The interaction of RasGAP and p190 RhoGAP in two multiprotein complexes could constitute an additional level of Rho regulation during morphogenetic events of gastrulation. |
Databáze: | OpenAIRE |
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