SOS1 Proteine (SOS1)

Human Son of Sevenless Homolog 1 (Drosophila) (SOS1) Interaktionspartner

1. Findings identified p.Ser548Arg missense mutation in Son of Sevenless Homolog 1 (SOS1) in the boy, confirmed in his mother.

2. We report on a novel pathogenic mutation in the SOS1 gene and a large clinical spectrum in a Noonan syndrome family with ten genetically confirmed affected individuals.

3. Data indicate dynamic of H-Ras (zeige HRAS Proteine) functional cycle as controlled by son of sevenless homolog 1 (Sos).

4. In summary, patients from two families with history of non-syndromic autosomal-dominant HGF (zeige HGF Proteine) from Malopolska and Mazovia provinces in Poland had not been affected by HGF (zeige HGF Proteine) type 1, caused by a single-cytosine insertion in exon 21 of the SOS-1 gene.

5. Mutation scanning of the entire coding sequence of SOS1 gene identified seven intronic variants and one new exonic substitution (c.138G > A). The seven common intronic variants were not considered to be of pathogenic importance. The exonic substitution c.138G > A was found to be absent in 100 ethnically matched normal control chromosomes, not expected to have functional significance based on prediction bioinformatics tool

6. Grb2-independent interactions are sufficient to retain human SOS on the membrane for many minutes, during which a single SOS molecule could processively activate thousands of Ras molecules.

7. a computational methodology that overlays any variant database onto the somatic mutations in all cancer exomes identified activating SOS1 mutations associated with Noonan syndrome as significantly altered in melanoma

8. Data show that a heterozygous son of sevenless homolog 1 (SOS1) gene frameshift mutation (c.3266dup or c.3248dup) was identified in each patient.

9. The present study provides a first evidence of allelic imbalance of SOS1 and pinpoints this condition as a possible mechanism underlying a different penetrance of some SOS1-mutated alleles in unrelated carriers

10. In non-apoptotic cells, nuclear EGFR (zeige EGFR Proteine) induced SOS1 expression by directly binding to the SOS1 promoter.

Mouse (Murine) Son of Sevenless Homolog 1 (Drosophila) (SOS1) Interaktionspartner

1. a direct mechanistic link between Sos1 and control of intracellular oxidative stress, and demonstrate functional prevalence of Sos1 over Sos2 with regards to cellular proliferation and viability.

2. findings suggest that targeting the Src (zeige SRC Proteine)/Abl (zeige ABL1 Proteine)/Sos1/Rac (zeige AKT1 Proteine) pathway may represent a double-edged sword to control both cancer-invasive capacities and cancer-related inflammation.

3. The increased activity of the PI3K/AKT (zeige AKT1 Proteine) pathway led to downregulation of the surface receptor CD62L (zeige SELL Proteine) in Sos-1/2dKO T cells and a subsequent impairment in T-cell migration.

4. SUMOylation of Grb2 (zeige GRB2 Proteine) enhances the ERK (zeige EPHB2 Proteine) activity by increasing its binding with Sos1.

5. Data suggest that interactions between Sos1 (Son of Sevenless homolog 1) and Crk (zeige CRK Proteine) (proto-oncogene (zeige RAB1A Proteine) proteins c-crk (zeige CRK Proteine)) involve electrostatic interactions at binding sites.

6. ROS1 kinase activity and MEK1/2-ERK1/2 signaling regulates epithelial differentiation in the epididymis.

7. Sos1 has distinct roles in acting as a scaffold to oligomerize the adaptor protein LAT (zeige LAT Proteine), and in guanine nucleotide exchange activity

8. ezrin also is important for the activity of SOS itself. Ezrin interacts with GDP-Ras and with the Dbl homology (DH)/pleckstrin homology (PH) domains of SOS, bringing GDP-Ras to the proximity of the allosteric site of SOS.

9. Absolute counts of mature B and T cells in spleen and peripheral blood were unchanged in single-knockout mutants, while significantly reduced in Sos1/2 double-knockout mice.

10. Study shows that the ability of Sos1/Grb2 to appropriately regulate pluripotency and differentiation factors and to initiate primitive endoderm development requires collective binding of multiple Sos1/Grb2 domains to their protein and phospholipid ligands.