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High AJUBA level enhances cervical cancer cells.
Data show that AJUBA upregulated MMP10 (Montrer MMP10 Protéines) and MMP13 (Montrer MMP13 Protéines) expression in esophageal squamous cell carcinoma (ESCC).
Mechanistic investigations reveal that AJUBA specifically binds the FERM domain of JAK1 (Montrer JAK1 Protéines) to dissociate JAK1 (Montrer JAK1 Protéines) from the IFNgamma recepter, resulting in an inhibition of STAT1 (Montrer STAT1 Protéines) phosporylation and concomitantly its nuclear translocation. Clinically, the level of AJUBA in CRC (Montrer CALR Protéines) specimens is negatively correlated with the levels of IFIT2 (Montrer IFIT2 Protéines) and pSTAT1
AJUBA is a LIM domain protein and contributes to the formation and stability of cadherin-mediated cell-cell adhesion. Loss of AJUBA enhances Prostate cancer cell migration and downregulation of AJUBA expression is observed in metastatic Prostate cancer.
Mutations of the LIM protein AJUBA mediate sensitivity of head and neck squamous cell carcinomas to treatment with PLK1 inhibitors.
mitotic phosphorylation of Ajuba is sufficient to promote cell proliferation and anchorage-independent growth in vitro and tumorigenesis in vivo
The results in this study uncovered that JUB was a regulator involved in proliferation of glioma cells, and it could be used as a potential therapeutic target for glioma.
AJUBA negatively regulates YAP activity through the LATS family, and inactivation of AJUBA is a novel key mechanism in malignant mesothelioma cell proliferation
the LIM protein JUB serves as a tumor-promoting gene in colorectal cancer by promoting epithelial-mesenchymal transition, a critical process of metastasis.
The LIM (Montrer PDLIM5 Protéines) domain of Ajuba can competitively bind to the N-terminal of Aurora-A (Montrer AURKA Protéines), and inhibited the interaction between N-terminal and C-terminal of Aurora A (Montrer AURKA Protéines).
Ajuba recruits p300/CBP (Montrer CREBBP Protéines) via its LIM (Montrer PDLIM5 Protéines) domain and facilitates p300/CBP (Montrer CREBBP Protéines) binding to PPARg (Montrer PPARG Protéines). Moreover, Ajuba, PPARg (Montrer PPARG Protéines), p300/CBP (Montrer CREBBP Protéines) can cooperatively occupy the PPARg (Montrer PPARG Protéines) target promoters and concomitantly increases histone acetylation at these loci.
Ajuba is a novel coactivator for liver X receptors and may play important role in lipid and glucose metabolism.
Findings support the importance of adhesion molecules (VE-cadherin and CD31), survivin, and Ajuba in modulating the Hippo pathway, which regulates, in part, proliferation and survival in hemangioendotheliomas.
PKD1-mediated phosphorylation of SNAI1 occurs in the nucleus and generates a nuclear, inactive DNA/SNAI1 complex that shows decreased interaction with its co-repressor Ajuba.
This paper presents evidence indicating that the human and mouse Ajuba is a new cytosolic component of the IL-1 (Montrer IL1A Protéines) signaling pathway, influencing the assembly and activity of the aPKC/p62 (Montrer GTF2H1 Protéines)/TRAF6 (Montrer TRAF6 Protéines) multiprotein signaling complex.
identification of the protein arginine methyltransferase 5 (PRMT5 (Montrer PRMT5 Protéines)) as an effector recruited to SNAIL (Montrer SNAI1 Protéines) through an interaction with AJUBA that functions to repress the SNAIL (Montrer SNAI1 Protéines) target gene, E-cadherin (Montrer CDH1 Protéines)
cytoplasmic LIM protein that binds glial glutamate transporter GLT-1 and is proposed to allow glial glutamate transporter GLT-1 to regulate intracellular signaling or interact with the cytoskeleton
LIM domain-containing protein ajuba
, jub, ajuba homolog
, protein ajuba
, Ajuba protein
, ajuba homolog