المؤلفون: Jennifer Aurandt, Kun-Liang Guan, Yi Rao, Claudia Jürgensen, Weiquan Li

المصدر: Journal of Cell Science. 132

مصطلحات موضوعية: animal structures, Kinase, fungi, Cell, Tyrosine phosphorylation, Cell Biology, Biology, Molecular biology, Article, Blot, chemistry.chemical_compound, medicine.anatomical_structure, nervous system, chemistry, embryonic structures, Netrin, medicine, Proto-oncogene tyrosine-protein kinase Src

الوصف: During neuronal development, netrin and its receptors UNC5 and DCC (deleted in colorectal cancer) guide axonal growth cones in navigating to their targets. Netrin also plays important roles in the regulation of cell migration, tissue morphogenesis and tumor growth. Here, we show that netrin induces UNC5 tyrosine phosphorylation and that this effect of netrin is dependent on its co-receptor DCC. UNC5 tyrosine phosphorylation is known to be important for netrin to induce cell migration and axonal repulsion. Src tyrosine kinase activity is required for netrin to stimulate UNC5 tyrosine phosphorylation in neurons and transfected cells. The SH2 domain of Src kinase directly interacts with the cytosolic domain of UNC5 in a tyrosine-phosphorylation-dependent manner. Furthermore, the tyrosine kinase focal adhesion kinase (FAK) is also involved in netrin-induced UNC5 tyrosine phosphorylation. Both Src and FAK can phosphorylate UNC5. Our data suggest a model in which netrin stimulates UNC5 tyrosine phosphorylation and signaling in a manner dependent on the co-receptor DCC, through the recruitment of Src and FAK kinases.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::906a22b63f8d40ae58f7273e4c2907bbTest
https://doi.org/10.1242/jcs.230342Test

المؤلفون: Weiquan, Li, Jennifer, Aurandt, Claudia, Jürgensen, Claudia, Jürgense, Yi, Rao, Kun-Liang, Guan

المصدر: Journal of Cell Science. 119:47-55

مصطلحات موضوعية: animal structures, Receptors, Cell Surface, Protein tyrosine phosphatase, SRC Family Tyrosine Kinase, SH2 domain, Article, Receptor tyrosine kinase, SH3 domain, Mice, chemistry.chemical_compound, Netrin, Animals, Humans, Nerve Growth Factors, Phosphorylation, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cells, Cultured, Neurons, biology, Tumor Suppressor Proteins, fungi, Tyrosine phosphorylation, Cell Biology, Netrin-1, Protein Structure, Tertiary, Cell biology, src-Family Kinases, nervous system, chemistry, Focal Adhesion Protein-Tyrosine Kinases, embryonic structures, biology.protein, Cancer research, Tyrosine, Signal Transduction, Proto-oncogene tyrosine-protein kinase Src

الوصف: During neuronal development, netrin and its receptors UNC5 and DCC (deleted in colorectal cancer) guide axonal growth cones in navigating to their targets. Netrin also plays important roles in the regulation of cell migration, tissue morphogenesis and tumor growth. Here, we show that netrin induces UNC5 tyrosine phosphorylation and that this effect of netrin is dependent on its co-receptor DCC. UNC5 tyrosine phosphorylation is known to be important for netrin to induce cell migration and axonal repulsion. Src tyrosine kinase activity is required for netrin to stimulate UNC5 tyrosine phosphorylation in neurons and transfected cells. The SH2 domain of Src kinase directly interacts with the cytosolic domain of UNC5 in a tyrosine-phosphorylation-dependent manner. Furthermore, the tyrosine kinase focal adhesion kinase (FAK) is also involved in netrin-induced UNC5 tyrosine phosphorylation. Both Src and FAK can phosphorylate UNC5. Our data suggest a model in which netrin stimulates UNC5 tyrosine phosphorylation and signaling in a manner dependent on the co-receptor DCC, through the recruitment of Src and FAK kinases.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2124a8f64944b128dcc0bb5ff0a652aTest
https://doi.org/10.1242/jcs.02697Test