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This study indicates that CISH functions as a conserved in vivo target and regulator of STAT5 (show STAT5B Proteins) in the control of embryonic hematopoiesis.
the type II SOCS genes (CISH, SOCS1 (show SOCS1 Proteins)-3) are particularly relevant to immune regulation in fish
CIS interacted with phosphorylated EpoR (show EPOR Proteins) at Y401, which was critical for the activation of STAT5 (show STAT5A Proteins) and ERK (show EPHB2 Proteins).
Studies indicate that suppressors of cytokine signaling (SOCS) proteins CIS, SOCS1 (show SOCS1 Proteins), and SOCS3 (show SOCS3 Proteins) can be considered the third immunocheckpoint molecules since they regulate cytokine signals that control the polarization of CD4 (show CD4 Proteins)(+) T cells and the maturation of CD8 (show CD8A Proteins)(+) T cells.
CISH rs414171 and rs6768300 variants might be associated with protection from pulmonary tuberculosis in Zahedan, Southeast Iran.
This study showed that there was significantly increased levels of CIS mRNA in elderly and Alzheimer's disease brains.
Data indicate that CIS protein stability is regulated through multiple mechanisms, including ubiquitination and interaction with Elongin B (show TCEB2 Proteins)/C proteins, whereas CIS functional inhibition of PRLR (show PRLR Proteins) signaling is dependent on the Elongin B (show TCEB2 Proteins)/C interaction.
SOCS single nucleotide polymorphism is associated with breast cancer.
Study in Chinese Han population confirms that previously identified variants of CISH are associated with susceptibility to pulmonary tuberculosis.
CISH gene polymorphisms at -292 (rs414171) are associated with HBV clearance in HBeAg-positive CHB patients in the immune active phase, and AA is a favorable genotype for this effect.
Two SNPs (rs414171 and rs2239751) in the CISH gene were associated with persistent HBV infection in Han Chinese population
two genetic variants in CISH gene appear to increase susceptibility to TB in Chinese Han population
CISH mediates control of M. tuberculosis in mice early after infection via regulation of innate immune mechanisms.
this study identifies CIS as a critical negative regulator of IL-15 (show IL15 Proteins) signaling in NK cells
Data show that cytokine inducible SH2-containing protein Cish is induced upon T cell receptor stimulation and in the tumor microenvironment.
Results show that CISH has no non-redundant functions in beta cell proliferation or glucose homeostasis during pregnancy in mice. Socs2 (show SOCS2 Proteins) might compensate for the loss of Cish during pregnancy.
CIS has a critical role in controlling the proallergic generation of helper T cells.
CISH expression at the later stage of dendritic cell development triggers the shutdown of DC progenitor cell proliferation and facilitates DC differentiation into a potent stimulator of CTLs.
CIS and SOCS3 (show SOCS3 Proteins) play a role as negative feedback inhibitors of PRL (show PRL Proteins) action; Inhibition of CIS and SOCS3 (show SOCS3 Proteins) expression by glucocorticoids contributes to the positive effect of glucocorticoids on PRL (show PRL Proteins)-induced STAT5 (show STAT5A Proteins) activation.
Induction of CIS in response to EPO (show EPO Proteins) stimulation depends on Stat5 (show STAT5A Proteins) but not MAP kinase (show MAPK1 Proteins) or PI 3 (show PI3 Proteins)-kinase. Overexpression negatively regulates EPO (show EPO Proteins)-mediated cell proliferation, Stat5 (show STAT5A Proteins) phosphorylation, & activation of a Stat (show STAT1 Proteins)-dependent luciferase reporter.
CIS negatively regulates signaling at two levels, apoptosis and proliferation, and thereby sets a threshold for signal transduction
The protein encoded by this gene contains a SH2 domain and a SOCS box domain. The protein thus belongs to the cytokine-induced STAT inhibitor (CIS), also known as suppressor of cytokine signaling (SOCS) or STAT-induced STAT inhibitor (SSI), protein family. CIS family members are known to be cytokine-inducible negative regulators of cytokine signaling. The expression of this gene can be induced by IL2, IL3, GM-CSF and EPO in hematopoietic cells. Proteasome-mediated degradation of this protein has been shown to be involved in the inactivation of the erythropoietin receptor. Multiple transcript variants encoding different isoforms have been found for this gene.
cytokine inducible SH2-containing protein
, cytokine-inducible SH2-containing protein
, cytokine inducible SH2 containing protein
, cytokine inducible SH2-containing protein A
, twinfilin, actin-binding protein, homolog 1, like
, Cytokine-inducible SH2-containing protein
, cytokine-inducible inhibitor of signaling type 1B
, suppressor of cytokine signaling
, cytokine-inducible SH2 protein
, cytokine inducible SH2-containing protein 1