High impact information on SOS2

• We have identified the guanine nucleotide exchange factors Sos1 and Sos2 as novel binding partners of Abi-1 [1].
• Pulse-chase experiments indicated that the half-life of Sos¿1 in NIH 3T3 cells was greater than 18 h, while that of Sos2 was less than 3 h [2].
• In the lysate, Sos2 and the two chimeric proteins could be stabilized by ATPgammaS [2].
• Evidence suggests that a protein kinase complex consisting of the myristoylated calcium-binding protein SOS3 and the serine/threonine protein kinase SOS2 is activated by a salt-stress-elicited calcium signal [3].
• Mammalian cells contain two related but distinct Sos proteins, Sos1 and Sos2 [4].

Biological context of SOS2

• To investigate this possibility, we have determined the chromosomal locations of both the mouse and the human Sos1 and Sos2 genes, using a combination of genetic linkage analysis and in situ hybridization to chromosomal spreads [5].
• 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 [6].

Anatomical context of SOS2

• Selected compounds were active against the growth of cultured cells from solid human tumors, i.e. Mck-7 breast effusion, lung A549 and lung MB-9812, bone SOS-2 and clear cell Caki renal tumor [7].

Analytical, diagnostic and therapeutic context of SOS2

• To gain insight into the in vivo function of sos2, we disrupted its catalytic CDC25-H domain by means of gene targeting techniques [8].

References