SOCS6 protein interacts with the phosphorylated Y568 in the juxtamembrane domain of c-Kit following SCF-stimulated tyrosine phosphorylation. Binding of SOCS6 to Y568 may mask this docking site for Src family kinases and this may inhibit the phosphorylation of p38 and ERK. This negatively regulates c-Kit receptor proliferation signal but not SCF-induced chemotaxis (Bayle et al. 2004, Zadjali et al 2011). Binding of SOCS6 mediates recruitment of elongin B and C to form a ubiquitin E3 ligase complex that leads to ubiquitination of KIT and its degradation (Zadjali et al 2011).