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we unveil a unique participation of Ajuba in maintaining CdGAP in an inactivated status to modulate Rac1 activity and stabilize junctions.
High AJUBA level enhances cervical cancer cells.
Data show that AJUBA upregulated MMP10 and MMP13 expression in esophageal squamous cell carcinoma (ESCC).
Mechanistic investigations reveal that AJUBA specifically binds the FERM domain of JAK1 to dissociate JAK1 from the IFNgamma recepter, resulting in an inhibition of STAT1 phosporylation and concomitantly its nuclear translocation. Clinically, the level of AJUBA in CRC specimens is negatively correlated with the levels of IFIT2 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 domain of Ajuba can competitively bind to the N-terminal of Aurora-A, and inhibited the interaction between N-terminal and C-terminal of Aurora A.
A Rac-PAK1-Ajuba feedback loop integrates spatiotemporal signaling with actin remodeling at cell-cell contacts and stabilizes preassembled cadherin complexes.
Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors and rexinoid receptor subtypes.
Ajuba contributes to the bridging of the cadherin adhesive complexes to the actin cytoskeleton and as such contribute to the formation or strengthening of cadherin-mediated cell-cell adhesion.
in addition to its effects upon Rac activity, Ajuba can also influence cell migration through regulation of PI(4,5)P2 synthesis through direct activation of PIPKIalpha enzyme activity
Ajuba is a new cytosolic component of the IL-1 signaling pathway modulating IL-1-induced NF-kappaB activation by influencing the assembly and activity of the aPKC/p62/TRAF6 multiprotein signaling complex
Ajuba promoted GSK-3beta-mediated phosphorylation of beta-catenin by reinforcing the association between beta-catenin and GSK-3beta.
Ajuba is a microtubule-associated protein that collaborates with Aurora B and BUBR1 at the metaphase-anaphase transition and this may be important to ensure proper chromosome segregation.
Ajuba is utilized as a corepressor selectively on Gfi1 target genes
Ajuba recruits p300/CBP via its LIM domain and facilitates p300/CBP binding to PPARg. Moreover, Ajuba, PPARg, p300/CBP can cooperatively occupy the PPARg 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 signaling pathway, influencing the assembly and activity of the aPKC/p62/TRAF6 multiprotein signaling complex.
identification of the protein arginine methyltransferase 5 (PRMT5) as an effector recruited to SNAIL through an interaction with AJUBA that functions to repress the SNAIL target gene, E-cadherin
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