ArticleMolecular and cellular biology1993
PU.1 is a component of a multiprotein complex which binds an essential site in the murine immunoglobulin lambda 2-4 enhancer.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed.
- Dendritic cell subsets and implications for cancer immunotherapy.Frontiers in immunology · 2024Review
- A novel molecular class that recruits HDAC/MECP2 complexes to PU.1 motifs reduces neuroinflammation.The Journal of experimental medicine · 2023Article
- Temporal analyses reveal a pivotal role for sense and antisense enhancer RNAs in coordinate immunoglobulin lambda locus activation.Nucleic acids research · 2023Article
- IRF4 as an Oncogenic Master Transcription Factor.Cancers · 2022Review
- Pharmacological inhibition of the transcription factor PU.1 in leukemia.The Journal of clinical investigation · 2017Article
- Restoring PU.1 induces apoptosis and modulates viral transactivation via interferon-stimulated genes in primary effusion lymphoma.Oncogene · 2017Article
- Article
- Pharmacologic efficacy of PU.1 inhibition by heterocyclic dications: a mechanistic analysis.Nucleic acids research · 2016Article
- The generation of antibody-secreting plasma cells.Nature reviews. Immunology · 2015Review
- Quantitative Investigation of Protein-Nucleic Acid Interactions by Biosensor Surface Plasmon Resonance.Methods in molecular biology (Clifton, N.J.) · 2015Article
- The transcription factors IRF8 and PU.1 negatively regulate plasma cell differentiation.The Journal of experimental medicine · 2014Article
- Mechanistic heterogeneity in site recognition by the structurally homologous DNA-binding domains of the ETS family transcription factors Ets-1 and PU.1.The Journal of biological chemistry · 2014Article
- Structure-dependent inhibition of the ETS-family transcription factor PU.1 by novel heterocyclic diamidines.Nucleic acids research · 2014Article
- Probing the electrostatics and pharmacological modulation of sequence-specific binding by the DNA-binding domain of the ETS family transcription factor PU.1: a binding affinity and kinetics investigation.Journal of molecular biology · 2013Article
- Transcription-coupled eviction of histones H2A/H2B governs V(D)J recombination.The EMBO journal · 2013Article
- Sequence discrimination by DNA-binding domain of ETS family transcription factor PU.1 is linked to specific hydration of protein-DNA interface.The Journal of biological chemistry · 2012Article
- A developmentally controlled competitive STAT5-PU.1 DNA binding mechanism regulates activity of the Ig κ E3' enhancer.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Mechanisms establishing TLR4-responsive activation states of inflammatory response genes.PLoS genetics · 2011Article
- NF-kappaB down-regulates expression of the B-lymphoma marker CD10 through a miR-155/PU.1 pathway.The Journal of biological chemistry · 2011Article
- The role of PU.1 and GATA-1 transcription factors during normal and leukemogenic hematopoiesis.Leukemia · 2010Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
B-cell-specific enhancers have been identified in the immunoglobulin lambda locus 3' of each constant-region cluster. These enhancers contain two distinct domains, lambda A and lambda B, which are essential for enhancer function. lambda B contains a near-consensus binding site for the Ets family of transcription factors. In this study, we have identified a B-cell-specific protein complex which binds the lambda B motif of the lambda 2-4 enhancer in vitro and appears necessary for the activity of the enhancer in vivo, since mutations in lambda B which prevent this interaction also eliminate enhancer function. This complex contains PU.1, a member of the Ets family, and a transcriptional activator whose expression is restricted to cells of the hematopoietic system with the exception of T lymphocytes. In addition, it contains a factor which binds specifically to a region adjacent to the PU.1 binding site. This factor cannot bind lambda B autonomously but appears to require interaction with the PU.1 protein to stabilize its association with the DNA. This complex may be identical or related to the PU.1/NF-EM5 complex which interacts with a homologous DNA element in the immunoglobulin kappa 3' enhancer.
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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.