Hipk2
Mostrando 1-10 de 10 artigos, teses e dissertações.
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1. Functional study of HIPK2 during development / Estudo de função de HIPK2 durante o desenvolvimento embrionário
HIPK2 (homeodomain interacting protein kinase 2) é uma proteína quinase nuclear, originalmente identificada por interagir com homeoproteínas. Sua atividade quinase contribui para a regulação de diversas vias, ativando o programa de morte celular em resposta a estímulos externos ou promovendo diferenciação celular por atuar como co-fator de homeoprote
Publicado em: 2007
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2. US11 of Herpes Simplex Virus Type 1 Interacts with HIPK2 and Antagonizes HIPK2-Induced Cell Growth Arrest
Homeodomain-interacting protein kinase 2 (HIPK2) is a nuclear serine/threonine kinase of the subfamily of dual-specificity Yak1-related kinase proteins. HIPK2 was first described as a homeodomain-interacting protein kinase acting as a corepressor for homeodomain transcription factors. More recently, it was reported that HIPK2 plays a role in p53-mediated cel
American Society for Microbiology.
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3. Covalent modification of the homeodomain-interacting protein kinase 2 (HIPK2) by the ubiquitin-like protein SUMO-1
Posttranslational modifications such as ubiquitination and phosphorylation play an important role in the regulation of cellular protein function. Homeodomain-interacting protein kinase 2 (HIPK2) is a member of the recently identified family of nuclear protein kinases that act as corepressors for homeodomain transcription factors. Here, we show that HIPK2 is
The National Academy of Sciences.
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4. Homeodomain-interacting protein kinase-2 mediates CtBP phosphorylation and degradation in UV-triggered apoptosis
Homeodomain-interacting protein kinase-2 (HIPK2) is a serine/threonine kinase involved in transcriptional regulation and apoptosis. The transcriptional corepressor CtBP (carboxyl-terminal binding protein) also plays a fundamental role in these processes. Our previous studies indicate that HIPK2 participates in a pathway of UV-triggered CtBP clearance that re
National Academy of Sciences.
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5. Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation
Axin and p53 are tumor suppressors, controlling cell growth, apoptosis, and development. We show that Axin interacts with homeodomain-interacting protein kinase-2 (HIPK2), which is linked to UV-induced p53-dependent apoptosis by interacting with, and phosphorylating Ser 46 of, p53. In addition to association with p53 via HIPK2, Axin contains a separate domai
Nature Publishing Group.
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6. Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)
The tumor suppressor p53 is regulated in part by binding to cellular proteins. We used p53 as bait in the yeast two-hybrid system and isolated homeodomain-interacting protein kinase 1 (HIPK1) as a p53-binding protein. Deletion analysis showed that amino acids 100–370 of p53 and amino acids 885-1093 of HIPK1 were sufficient for HIPK1–p53 interaction. HIPK
The National Academy of Sciences.
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7. Wnt-1 signal induces phosphorylation and degradation of c-Myb protein via TAK1, HIPK2, and NLK
The c-myb proto-oncogene product (c-Myb) regulates both the proliferation and apoptosis of hematopoietic cells by inducing the transcription of a group of target genes. However, the biologically relevant molecular mechanisms that regulate c-Myb activity remain unclear. Here we report that c-Myb protein is phosphorylated and degraded by Wnt-1 signal via the p
Cold Spring Harbor Laboratory Press.
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8. Alterations of BRAF and HIPK2 loci predominate in sporadic pilocytic astrocytoma
American Academy of Neurology.
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9. HIPK2 overexpression leads to stabilization of p53 protein and increased p53 transcriptional activity by decreasing Mdm2 protein levels
BioMed Central.
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10. Stress-dependent Daxx-CHIP Interaction Suppresses the p53 Apoptotic Program*♦
Our previous studies have implicated CHIP (carboxyl terminus of Hsp70-interacting protein) as a co-chaperone/ubiquitin ligase whose activities yield protection against stress-induced apoptotic events. In this report, we demonstrate a stress-dependent interaction between CHIP and Daxx (death domain-associated protein). This interaction interferes with the str
American Society for Biochemistry and Molecular Biology.