ArticleMolecular and cellular biology1996
p95vav associates with the nuclear protein Ku-70.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 79 citations in OpenAlex.
- Ezh2 harnesses the intranuclear actin cytoskeleton to remodel chromatin in differentiating Th cells.iScience · 2021Article
- VAV2 is required for DNA repair and implicated in cancer radiotherapy resistance.Signal transduction and targeted therapy · 2021Article
- Article
- SCF(FBXW7)-mediated degradation of p53 promotes cell recovery after UV-induced DNA damage.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Mechanism and function of Vav1 localisation in TCR signalling.Journal of cell science · 2012Article
- The distinct role of guanine nucleotide exchange factor Vav1 in Bcl-2 transcription and apoptosis inhibition in Jurkat leukemia T cells.Acta pharmacologica Sinica · 2011Article
- Article
- DNase I-resistant DNA-dependent protein kinase activity in Xenopus oocytes.Molecular and cellular biochemistry · 2008Article
- Deletion of Ku70, Ku80, or both causes early aging without substantially increased cancer.Molecular and cellular biology · 2007Article
- An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligand.Cell communication and signaling : CCS · 2006Article
- Article
- Vav1 is a component of transcriptionally active complexes.The Journal of experimental medicine · 2002Article
- Solution structure of N-terminal SH3 domain of Vav and the recognition site for Grb2 C-terminal SH3 domain.Journal of biomolecular NMR · 2002Article
- Inhibition of Ku heterodimer DNA end binding activity during granulocytic differentiation of human promyelocytic cell lines.Oncogene · 2001Article
- Human securin, hPTTG, is associated with Ku heterodimer, the regulatory subunit of the DNA-dependent protein kinase.Nucleic acids research · 2001Article
- Article
- The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH(2)-terminal kinase 1.The Journal of experimental medicine · 2000Article
- Hypermethylation of metallothionein-I promoter and suppression of its induction in cell lines overexpressing the large subunit of Ku protein.The Journal of biological chemistry · 1999Article
- Ku antigen-DNA conformation determines the activation of DNA-dependent protein kinase and DNA sequence-directed repression of mouse mammary tumor virus transcription.Molecular and cellular biology · 1999Article
- hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways.Molecular and cellular biology · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proto-oncogene vav is expressed solely in hematopoietic cells and plays an important role in cell signaling, although little is known about the proteins involved in these pathways. To gain further information, the Src homology 2 (SH2) and 3 (SH3) domains of Vav were used to screen a lymphoid cell cDNA library by the yeast two-hybrid system. Among the positive clones, we detected a nuclear protein, Ku-70, which is the DNA-binding element of the DNA-dependent protein kinase. In Jurkat and UT7 cells, Vav is partially localized in the nuclei, as judged from immunofluorescence and confocal microscopy studies. By using glutathione S-transferase fusion proteins derived from Ku-70 and coimmunoprecipitation experiments with lysates prepared from human thymocytes and Jurkat and UT7 cells, we show that Vav associates with Ku-70. The interaction of Vav with Ku-70 requires only the 150-residue carboxy-terminal portion of Ku-70, which binds to the 25 carboxy-terminal residues of the carboxy SH3 domain of Vav. A proline-to-leucine mutation in the carboxy SH3 of Vav that blocks interaction with proline-rich sequences does not modify the binding of Ku-70, which lacks this motif. Therefore, the interaction of Vav with Ku-70 may be a novel form of protein-protein interaction. The potential role of Vav/Ku-70 complexes is discussed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.