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PMID: 17070092,15690087
We have also shown that SOCS2 binds Elongin B and C</csml:comment>
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<csml:comment type="text">


PMID: 17070092,15690087
We have also shown that SOCS2 binds Elongin B and C</csml:comment>
</csml:comments>
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<csml:comment type="text">

</csml:comment>
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<csml:comment type="text">


PMID: 17070092,10433229,9430658,10998044
GH induces the expression of several members of the SOCS family, including SOCS2</csml:comment>
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<csml:comment type="text">


indirect</csml:comment>
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</csml:comment>
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<csml:comment type="text">


PMID: 17070092,10433229,9430658,10998044
GH induces the expression of several members of the SOCS family, including SOCS2</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">


indirect</csml:comment>
</csml:comments>
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PMID: 17070092,15125881
SOCS2 overexpression in vitro shows a partial inhibition of GH-dependent signaling (e.g. phosphorylation of STAT5 and JAK2, DNA-binding capacity of STAT5 and GH-dependent reporter activity), in contrast to SOCS1 and SOCS3, which have a stronger inhibitory action</csml:comment>
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PMID: 17070092,15125881
SOCS2 overexpression in vitro shows a partial inhibition of GH-dependent signaling (e.g. phosphorylation of STAT5 and JAK2, DNA-binding capacity of STAT5 and GH-dependent reporter activity), in contrast to SOCS1 and SOCS3, which have a stronger inhibitory action</csml:comment>
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PMID: 17070092,15125881
SOCS2 overexpression in vitro shows a partial inhibition of GH-dependent signaling (e.g. phosphorylation of STAT5 and JAK2, DNA-binding capacity of STAT5 and GH-dependent reporter activity), in contrast to SOCS1 and SOCS3, which have a stronger inhibitory action

PMID: 17070092,1058543
It has also been shown that SOCS2 can inhibit JAK2 tyrosine phosphorylation even in the absence of the GH receptor 
</csml:comment>
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PMID: 17070092
SOCS2 is able to bind the GH receptor through tyrosines Y595 and Y487</csml:comment>
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PMID: 17070092
These results suggest that SOCS2 might act as a ubiquitin ligase, promoting the ubiquitination and degradation of the GH receptor.</csml:comment>
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PMID: 17070092
These results suggest that SOCS2 might act as a ubiquitin ligase, promoting the ubiquitination and degradation of the GH receptor.</csml:comment>
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PMID: 17070092,9727029,10747872
SOCS2 binds the IGF-1 receptor and inhibits IGF-1-induced STAT3 activation</csml:comment>
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indirect</csml:comment>
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PMID: 17070092,9727029,10747872
SOCS2 binds the IGF-1 receptor and inhibits IGF-1-induced STAT3 activation</csml:comment>
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PMID: 17070092,9727029,10747872
SOCS2 binds the IGF-1 receptor and inhibits IGF</csml:comment>
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indirect</csml:comment>
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PMID:17070092,15831713
Indeed, recent findings have demonstrated that SOCS2 has inhibitory effects on both GH and IGF-1 stimulation of collagen expression in intestinal mesenchymal cells

</csml:comment>
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indirect</csml:comment>
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PMID:17070092,15831713
Indeed, recent findings have demonstrated that SOCS2 has inhibitory effects on both GH and IGF-1 stimulation of collagen expression in intestinal mesenchymal cells

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<csml:comment type="text">

</csml:comment>
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<csml:comment type="text">


PMID: 17070092
SOCS2 expression is induced by PRL in several systems</csml:comment>
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<csml:comment type="text">


indirect</csml:comment>
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<csml:comment type="text">


PMID: 17070092
SOCS2 expression is induced by PRL in several systems</csml:comment>
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</csml:comment>
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<csml:comment type="text">


PMID: 17070092,10455112
It has also been shown that SOCS2 is able to bind the PRL receptor </csml:comment>
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<csml:comment type="text">

</csml:comment>
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<csml:comment type="text">


indirect</csml:comment>
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<csml:comments>
<csml:comment type="text">

indirect</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">

indirect</csml:comment>
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PMID: 17070092,16199887
Similar studies show that SOCS2 enhances IL-2 and IL-3-dependent signaling through the degradation of SOCS3

PMID: 17070092
The degradation of SOCS3 by SOCS2 is enhanced by coexpression with Elongin BC and requires an intact SOCS box, suggesting that SOCS2 acts as a ubiquitin ligase towards SOCS3.</csml:comment>
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PMID: 17070092,9266833,12396724,14764607
 SOCS2 is able to downregulate the apoptotic effect of LIF in M1 cells , to block the EPO-dependent reporter activity and cell proliferation, and to decrease EGF-dependent STAT5 phosphorylation in PC12 cells</csml:comment>
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indirect</csml:comment>
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PMID: 17070092,9266833,12396724,14764607
 SOCS2 is able to downregulate the apoptotic effect of LIF in M1 cells , to block the EPO-dependent reporter activity and cell proliferation, and to decrease EGF-dependent STAT5 phosphorylation in PC12 cells</csml:comment>
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PMID: 17070092
It has been shown that IL-10 inhibits IFN-alpha-dependent STAT1 activation, but up regulates SOCS2 and SOCS3 in liver.</csml:comment>
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PMID: 17070092
It has been shown that IL-10 inhibits IFN-alpha-dependent STAT1 activation, but up regulates SOCS2 and SOCS3 in liver.</csml:comment>
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PMID: 17070092
It has been shown that IL-10 inhibits IFN-alpha-dependent STAT1 activation, but up regulates SOCS2 and SOCS3 in liver.</csml:comment>
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PMID: 17070092
It has been shown that IL-10 inhibits IFN-alpha-dependent STAT1 activation, but up regulates SOCS2 and SOCS3 in liver.</csml:comment>
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PMID: 17070092
It has been shown that IL-10 inhibits IFN-alpha-dependent STAT1 activation, but up regulates SOCS2 and SOCS3 in liver.</csml:comment>
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PMID: 17070092
A recent study has also shown that SOCS2, as well as CIS, is able to bind the leptin receptor (LR) through specific phosphorylated tyrosines: Y985 and Y1077 for CIS and Y1077 for SOCS2.</csml:comment>
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PMID: 17070092
A recent study has also shown that SOCS2, as well as CIS, is able to bind the leptin receptor (LR) through specific phosphorylated tyrosines: Y985 and Y1077 for CIS and Y1077 for SOCS2.

PMID: 17070092,16684815
Interestingly, SOCS2 can block the access of CIS to Y985 on the receptor through interaction with the SOCS box of CIS, suggesting that SOCS2 might act as a ubiquitin ligase towards CIS</csml:comment>
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PMID: 17070092,16684815
Interestingly, SOCS2 can block the access of CIS to Y985 on the receptor through interaction with the SOCS box of CIS, suggesting that SOCS2 might act as a ubiquitin ligase towards CIS</csml:comment>
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PMID: 17070092,16415877
SOCS2 mRNA and protein were induced by lipoxin (LXA4), an eicosanoid mediator with potent anti-inflammatory properties, by activation of two receptors, AhR and LXAR, in dendritic cells (DC)</csml:comment>
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PMID: 17070092,16415877
SOCS2 mRNA and protein were induced by lipoxin (LXA4), an eicosanoid mediator with potent anti-inflammatory properties, by activation of two receptors, AhR and LXAR, in dendritic cells (DC)</csml:comment>
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PMID: 17070092,16415877
SOCS2 mRNA and protein were induced by lipoxin (LXA4), an eicosanoid mediator with potent anti-inflammatory properties, by activation of two receptors, AhR and LXAR, in dendritic cells (DC)</csml:comment>
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PMID: 17070092,16415877
SOCS2 mRNA and protein were induced by lipoxin (LXA4), an eicosanoid mediator with potent anti-inflammatory properties, by activation of two receptors, AhR and LXAR, in dendritic cells (DC)</csml:comment>
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PMID: 17070092
In acute myeloid leukemia cells, GM-CSF stimulates SOCS2, SOCS3, and procaspase 2 and 3 expression.</csml:comment>
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PMID: 17070092
Cytokine receptors act through a complex signaling network, involving Janus kinases (JAKs) and the signal transducers and activators of transcription (STATs), to regulate diverse biological processes which control growth, development, homeostasis and immune function, among others.</csml:comment>
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PMID: 17070092
This process involves oligomerization and activation of the JAK family of tyrosine kinases, which in turn phosphorylate the receptor at specific tyrosine residues.</csml:comment>
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PMID: 17070092
This process involves oligomerization and activation of the JAK family of tyrosine kinases, which in turn phosphorylate the receptor at specific tyrosine residues.</csml:comment>
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PMID: 17070092
STAT proteins are then recruited to these phosphorylated sites and are phosphorylated at tyrosine amino acids by the action of JAK proteins</csml:comment>
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PMID: 17070092
STAT proteins are then recruited to these phosphorylated sites and are phosphorylated at tyrosine amino acids by the action of JAK proteins</csml:comment>
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PMID: 17070092,15020666
Dimerization of the phosphorylated STATs leads to nuclear migration and regulation of gene expression </csml:comment>
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PMID: 17070092,15020666
Dimerization of the phosphorylated STATs leads to nuclear migration and regulation of gene expression </csml:comment>
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PMID: 17070092,15020666
Dimerization of the phosphorylated STATs leads to nuclear migration and regulation of gene expression </csml:comment>
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This process involves oligomerization and activation of the JAK family of tyrosine kinases, which in turn phosphorylate the receptor at specific tyrosine residues.</csml:comment>
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