Disease relevance of Sos2

• Immunohistochemical analysis for two of the most highly differentially expressed genes (prion and Sos2) demonstrated a correlation between the observed differential gene expression after traumatic brain injury and corresponding protein translation [1].

High impact information on Sos2

• To address the specificity or redundancy of these exchange factors, we have generated Sos1/Sos2 double- or RasGRP3-deficient B cell lines and determined their ability to mediate Ras activation upon B cell receptor (BCR) stimulation [2].
• The BCR requires RasGRP3; in contrast, epidermal growth factor receptor is dependent on Sos1 and Sos2 [2].
• The mammalian sos1 and sos2 genes encode highly homologous members of the Son-of-sevenless family of guanine nucleotide exchange factors [3].
• Ras-guanine nucleotide exchange factor sos2 is dispensable for mouse growth and development [3].
• Mating among heterozygous sos2(+/-) mice produced viable sos2(-/-) offspring with a normal Mendelian pattern of inheritance, indicating that the loss of sos2 does not interfere with embryo viability in the uterus [3].

Biological context of Sos2

• We find that the murine Sos1 and Sos2 genes map to chromosomes 17E and 12C3.3-D and their human counterparts to chromosomes 2p21-2p2 and 14q21, respectively [4].
• Under specific conditions, the complex formed by the adaptor protein Grb2 and the guanine-nucleotide exchange factor Sos2 is responsible for the activation of Ras, a low-molecular-weight GTPase involved in the control of cell proliferation and differentiation [5].
• The vertebrate sos1 and sos2 gene products have a domain structurally related to the catalytic domain of the yeast CDC25NEF [6].
• The human SOS1 and SOS2 genes encode proteins that control GDP-->GTP exchange on ras proteins and are involved in signal transduction by tyrosine kinase receptors [7].

Anatomical context of Sos2

• In a myristoylated version, the chimeric gene encoding Sos2 at its C terminus made a stable protein in NIH 3T3 cells and induced focal transformation almost as efficiently as myr-msos1, while the myristoylated protein encoded by the other chimera was unstable and defective in the transformation assay [8].

Other interactions of Sos2

• Lysates of such desensitized cells were quantitatively immunoprecipitated with an antiserum recognizing both Sos1 and Sos2 proteins or a specific anti-Sos2 antiserum [9].
• The interaction between the N-terminal SH3 domain of the mouse Grb2 and one of its potential target sequences in the mouse, Sos2, a 15-residue peptide corresponding to residues 1264-1278, had been studied by NMR [5].

References