SOCS6 + Phosphopeptide
SOCS6 + Phosphopeptide: Human suppressor of cytokine signaling 6: SH2 complex with c-KIT phosphopeptide
PDB Code: 2VIF
The suppressor of cytokine signaling (SOCS) family comprises CIS1 and SOCS1-7. Members of this family are characterized by a SH2 substrate recognition domain and a C-terminal SOCS box which mediates assembly into ElonginBC-cullin ubiquitin ligase complexes. CIS1 and SOCS1-3 are well characterized as negative feedback inhibitors of cytokine receptor signaling via the JAK/STAT pathway, but the function of SOCS4-7 is less understood.
SOCS6 is ubiquitously expressed and is present in both the nuclear and cytoplasmic fractions. Transgenic mice overexpressing SOCS6 display improved glucose tolerance and insulin sensitivity similar to p85PI3K heterozygous mice. An insulin-dependent interaction between SOCS6 and the p85a subunit of the PI 3-Kinase was found, but its physiological importance is uncertain as SOCS6 knockout mice develop normally with the exception of a 10% reduction in body weight.
The SOCS6 SH2 domain preferentially binds to phosphopeptides containing a valine in the phosphotyrosine (pY) +1 position and a hydrophobic residue in the pY +2 and pY +3 positions. The in vivo interaction between SOCS6 and c-KIT (SCF receptor) was mapped to the juxtamembrane region pY568 site of c-KIT which matches the determined consensus (NGNN(pY)VYIDPT). This interaction was dependent on SCF-stimulation and decreased cell proliferation by reduced activation of ERK1/2 and p38, but did not inhibit activation of AKT or STATs. In order to gain insight into the substrate recognition of SOCS6 we determined the structure of the SOCS6 SH2 domain in complex with the c-KIT juxtamembrane tyrosine phosphorylated peptide at 1.45Å resolution.
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