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we determined the molecular mechanism responsible for IER3 degradation, involving a ternary complex of IER3, MDM2 (show MDM2 Proteins) and FHL2 (show FHL2 Proteins), which may contribute to cervical tumor growth. Furthermore, we demonstrated that FHL2 (show FHL2 Proteins) serves as a scaffold for E3 ligase and its substrate during the ubiquitination reaction, a function that has not been previously reported for this protein
Analysis of consensus EGR (show EGR1 Proteins)-binding elements (EBEs) showed that the immediate early response 3 gene (IER3) is a novel transcriptional target gene of EGR2 (show EGR2 Proteins) as confirmed by the luciferase assay, electrophoretic mobility-shift assay (EMSA), chromatin immunoprecipitation (ChIP), and western blot analysis.
Study characterized IEX-1's expression and function in rheumatoid arthritis synovial fibroblasts and showed that IEX-1 is highly expressed in RA-SFs and negatively regulates RA-SF activation.
interleukin-1beta (IL-1beta (show IL1B Proteins))-induced IER3 expression is mediated by the ERK1/2 target, transcription factor Elk-1 (show ELK1 Proteins).
findings suggest that IER3 is a putative tumor suppressor in the cervix, and the c-Ab1/p73beta/IER3 axis is a novel and crucial signaling pathway that confers etoposide chemosensitivity.
High expression of IER3 is associated with hepatocarcinoma.
In human samples removed from failed AVF, there was a significant increase in IEX-1 expression localized to the adventitia.
IEX-1 expression levels correlate with the severity of preeclampsia
Studied the binding effect of hcmv-miR (show MLXIP Proteins)-UL148D to the 3' untranslated region (3'UTR) of IEX-1.Results showed that only one binding site in the 3'UTR of IEX-1 was completely complementary to an 11nt sequence in the 5' terminus of hcmv-mir (show MLXIP Proteins)-UL148D.
the interference of IER3 with the PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins)-Fyn (show FYN Proteins) pathway represents a novel mechanism of Nrf2 (show GABPA Proteins) regulation that may get lost in tumors and by which IER3 exerts its stress-adaptive and tumor-suppressive activity.
IER3 expression is blunted during heart failure development in a titin (show TTN Proteins)-deficient mouse model.
these results indicate that IER3 is a key player in expanding the pool of APC (show APC Proteins) while highlighting the role of distinct effectors found in an obese microenvironment in this process
Loss of IEX-1 results in reduced VNH accompanied with a decrease in proliferation, reduced fibroblast, myofibroblast, and Ly6C staining accompanied with increased apoptosis mediated through a reduction in Vegf-A (show VEGFA Proteins)/Mcp-1 (show CPT1B Proteins) axis and Mmp-9 (show MMP9 Proteins).
IER3 supports KRASG12D-associated oncogenesis in the pancreas by sustaining ERK1/2 phosphorylation via phosphatase PP2A (show PPP2R2B Proteins) inhibition.
Stress-induced hematopoietic failure in the absence of immediate early (show JUN Proteins) response gene X-1 (IEX-1, IER3).
the interference of IER3 with the PI3K/Akt (show AKT1 Proteins)-Fyn (show FYN Proteins) pathway represents a novel mechanism of Nrf2 (show NFE2L2 Proteins) regulation that may get lost in tumors and by which IER3 exerts its stress-adaptive and tumor-suppressive activity.
IEX-1 has a role in activation of Erk (show EPHB2 Proteins) and NF-kB pathways, which affects thrombopoietin (show THPO Proteins)-promoted NHEJ DNA repair in hematopoietic stem cells
Data suggest a role for the immediate early (show JUN Proteins) response gene X-1 (IEX-1) in the control of colon epithelial homeostasis.
Our present investigation shows that null mutation of IEX-1 promotes differentiation of Th17 cells but compromises the survival of Th1 (show HAND1 Proteins) cells
IER3 plays a complex and to some extent contradictory role in cell cycle control and apoptosis. Effects of IER3 relate to an interference with certain signalling pathways
present data indicating that bovine IER3 is a strong regulator of immune-marker expression, specifically modulating bovine interleukin-8 (show IL8 Proteins) activation through the NF-kappaB (show NFKB1 Proteins)/IER3 pathway in response to the bovine viral diarrhea virus.
This gene functions in the protection of cells from Fas- or tumor necrosis factor type alpha-induced apoptosis. Partially degraded and unspliced transcripts are found after virus infection in vitro, but these transcripts are not found in vivo and do not generate a valid protein.
PACAP-responsive gene 1 protein
, anti-death protein
, differentiation-dependent gene 2 protein
, expressed in pancreatic carcinoma
, gly96, mouse, homolog of
, immediate early protein GLY96
, immediate early response 3 protein
, immediately early gene X-1
, protein DIF-2
, radiation-inducible immediate-early gene IEX-1
, cAMP inducible gene 3
, immediate early response 3
, ATP-binding cassette, sub-family F (GCN20), member 1