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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Ajuba LIM protein

Ajuba
Top mentioned proteins: LIM, CAN, V1a, Zyxin, Aurora
Papers on Ajuba
The LIM protein Ajuba promotes adipogenesis by enhancing PPARγ and p300/CBP interaction.
New
Hou et al., Shanghai, China. In Cell Death Differ, Jan 2016
Here, we report Ajuba is an important regulator of adipocyte differentiation by functioning as an obligate co-activator of PPARγ.
Ajuba Preferentially Binds LXRα/RXRγ Heterodimer to Enhance LXR Target Gene Expression in Liver Cells.
New
Hou et al., Shanghai, China. In Mol Endocrinol, Nov 2015
Here, we report that the LIM protein Ajuba binds to the hinge and the ligand binding domains of LXRα via its C-terminal tandem LIM motifs and enhances LXR target gene expression in liver cells.
Scalloped and Yorkie are required for cell cycle re-entry of quiescent cells after tissue damage.
New
Duronio et al., Chapel Hill, United States. In Development, Sep 2015
Ajuba, an upstream regulator of Hippo signaling that functions as a sensor of epithelial integrity, is also required for cell cycle re-entry.
JNK signaling is converted from anti- to pro-tumor pathway by Ras-mediated switch of Warts activity.
New
Igaki et al., Kyoto, Japan. In Dev Biol, Aug 2015
In contrast, in the presence of hyperactive Ras, JNK signaling enhances Yki activation by accumulating F-actin through the activity of the LIM domain protein Ajuba, thereby promoting tissue growth.
A hydrogel-endothelial cell implant mimics infantile hemangioma: modulation by survivin and the Hippo pathway.
New
Madri et al., New Haven, United States. In Lab Invest, Jul 2015
Consistent with the progression of a proliferative phase to an involuted phase, both the murine implants and human biopsy tissue exhibit reduced expression of Ajuba, YAP, and Survivin labeling as they progressed over time.
Ajuba proteins.
New
Longmore et al., Saint Louis, United States. In Curr Biol, Jul 2015
Schimizzi and Longmore summarise what we know about Ajuba LIM-domain proteins and their various subcellular roles.
Phenotype-genotype correlations of facial width and height proportions in patients with Class II malocclusion.
New
Southard et al., Iowa City, United States. In Orthod Craniofac Res, Apr 2015
OBJECTIVES: To characterize soft-tissue facial height and width variation in Class II malocclusion and test for correlations with genes HMGA2, AJUBA, and ADK.
Comprehensive genomic characterization of head and neck squamous cell carcinomas.
New
Impact
Cancer Genome Atlas Network, In Nature, Mar 2015
Other distinct subgroups contained loss-of-function alterations of the chromatin modifier NSD1, WNT pathway genes AJUBA and FAT1, and activation of oxidative stress factor NFE2L2, mainly in laryngeal tumours.
Genetic adaptations of the plateau zokor in high-elevation burrows.
Zhang et al., Kunming, China. In Sci Rep, 2014
response to hypoxia, oxygen homeostasis and erythrocyte homeostasis) are significantly enriched, are two genes, EPAS1 and AJUBA, involved in the response to hypoxia, where the parallel evolved sites are at positions that are highly conserved in sequence alignments from multiple species.
Genetic landscape of esophageal squamous cell carcinoma.
Impact
He et al., Beijing, China. In Nat Genet, 2014
The Hippo and Notch pathways were dysregulated by mutations in FAT1, FAT2, FAT3 or FAT4 (27%) or AJUBA (JUB; 7%) and NOTCH1, NOTCH2 or NOTCH3 (22%) or FBXW7 (5%), respectively.
Cytoskeletal tension inhibits Hippo signaling through an Ajuba-Warts complex.
Impact
Irvine et al., United States. In Cell, 2014
The influence of myosin activity on Yorkie depends genetically on the Ajuba LIM protein Jub, a negative regulator of Warts within the Hippo pathway.
The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.
Impact
Sharp et al., Nottingham, United Kingdom. In Nat Cell Biol, 2012
LIMD1 family member proteins Ajuba and WTIP also bind to VHL and PHDs 1 and 3, indicating that these LIM domain-containing proteins represent a previously unrecognized group of hypoxic regulators.
Protein kinase D1 maintains the epithelial phenotype by inducing a DNA-bound, inactive SNAI1 transcriptional repressor complex.
GeneRIF
Storz et al., Jacksonville, United States. In Plos One, 2011
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.
Ajuba is required for Rac activation and maintenance of E-cadherin adhesion.
GeneRIF
Braga et al., London, United Kingdom. In J Cell Biol, 2011
A Rac-PAK1-Ajuba feedback loop integrates spatiotemporal signaling with actin remodeling at cell-cell contacts and stabilizes preassembled cadherin complexes.
Retinoids regulate stem cell differentiation.
Review
Wagner et al., New York City, United States. In J Cell Physiol, 2011
Proteins that bind at or near RAREs include Sin3a, N-CoR1, PRAME, Trim24, NRIP1, Ajuba, Zfp423, and MN1/TEL.
LIM protein Ajuba functions as a nuclear receptor corepressor and negatively regulates retinoic acid signaling.
GeneRIF
Rauscher et al., Philadelphia, United States. In Proc Natl Acad Sci U S A, 2010
Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors and rexinoid receptor subtypes.
Ajuba: a new microtubule-associated protein that interacts with BUBR1 and Aurora B at kinetochores in metaphase.
GeneRIF
Birnbaum et al., Marseille, France. In Biol Cell, 2009
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 functions as a histone deacetylase-dependent co-repressor for autoregulation of the growth factor-independent-1 transcription factor.
GeneRIF
Grimes et al., Louisville, United States. In J Biol Chem, 2008
Ajuba is utilized as a corepressor selectively on Gfi1 target genes
[Aurora kinases and cancer].
Review
Okano et al., Gifu, Japan. In Gan To Kagaku Ryoho, 2005
Aurora A regulates centrosome function during M phase through its interactions with various cell cycle regulators including TACC, chTOG, Ajuba, BRCA1, LATS2, and p53.
Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells.
Impact
Saya et al., Kumamoto, Japan. In Cell, 2003
A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein.
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