Gene interactions and pathways from curated databases and text-mining

◀ Back to HRAS

HRAS — SOS2

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Sondermann et al., Cell 2004 : The recent discovery that Ras*GTP is an allosteric activator of SOS indicated that the regulation of SOS is more complex than originally envisaged
Langlois et al., J Biol Chem 1995 : Insulin and epidermal growth factor receptors transmit signals for cell proliferation and gene regulation through formation of active GTP bound p21ras mediated by the guanine nucleotide exchange factor Sos ... These data suggest that a negative feedback loop exists whereby activation of the Raf/MEK/MAP kinase cascade by p21ras causes Sos phosphorylation and, therefore, Sos/Grb2 dissociation, limiting the duration of p21ras activation by growth factors
Schneider et al., Eur J Immunol 1995 (Second Messenger Systems) : T cell antigen CD28 binds to the GRB-2/SOS complex, regulators of p21ras
D'Ambrosio et al., Eur J Immunol 1996 : In view of previous studies which demonstrated p21ras co-capping with ligated BCR, the data presented here suggest that Ig-alpha/beta- and SHC tyrosine phosphorylation dependent recruitment of the Grb2/Sos complex to the receptor can occur and may provide a mechanism by which the nucleotide exchange activity of Sos could mediate activation of BCR localized p21ras
Byrne et al., Oncogene 1996 (Pheochromocytoma) : p21Ras activation by the guanine nucleotide exchange factor Sos, requires the Sos/Grb2 interaction and a second ligand dependent signal involving the Sos N-terminus ... It has been suggested that a key event in growth factor induced p21Ras activation by the guanine nucleotide exchange factor Sos , is the recruitment of Sos to the plasma membrane by its interaction with the adaptor protein Grb2 ... To clarify the role of the Sos/Grb2 interaction in ligand stimulated p21Ras activation, we have utilised the observation that overexpression of the Sos C-terminal domain can effectively inhibit p21Ras dependent signalling in three different mammalian systems