ArticleProceedings of the National Academy of Sciences of the United States of America1997
The proliferation potential protein-related (P2P-R) gene with domains encoding heterogeneous nuclear ribonucleoprotein association and Rb1 binding shows repressed expression during terminal differentiation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- RBBP6 induces non-small cell lung cancer cell proliferation and high expression is associated with poor prognosis.Oncology letters · 2020Article
- The oncogenic potential of small nuclear ribonucleoprotein polypeptide G: a comprehensive and perspective view.American journal of translational research · 2019Review
- Expression analysis and association of RBBP6 with apoptosis in colon cancers.Journal of molecular histology · 2016Article
- The Drosophila retinoblastoma binding protein 6 family member has two isoforms and is potentially involved in embryonic patterning.International journal of molecular sciences · 2015Article
- RBBP6 isoforms regulate the human polyadenylation machinery and modulate expression of mRNAs with AU-rich 3' UTRs.Genes & development · 2014Article
- Article
- Solution structure of RING finger-like domain of retinoblastoma-binding protein-6 (RBBP6) suggests it functions as a U-box.The Journal of biological chemistry · 2012Article
- De-regulation of the RBBP6 isoform 3/DWNN in human cancers.Molecular and cellular biochemistry · 2012Article
- Modification by ubiquitin-like proteins: significance in apoptosis and autophagy pathways.International journal of molecular sciences · 2012Review
- Microarray analysis of Shigella flexneri-infected epithelial cells identifies host factors important for apoptosis inhibition.BMC genomics · 2010Article
- Systems genetics analyses predict a transcription role for P2P-R: molecular confirmation that P2P-R is a transcriptional co-repressor.BMC systems biology · 2010Article
- The RB/E2F pathway and regulation of RNA processing.Biochemical and biophysical research communications · 2009Review
- PACT is a negative regulator of p53 and essential for cell growth and embryonic development.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Characterization of Drosophila mini-me, a gene required for cell proliferation and survival.Genetics · 2006Article
- RNAs induced by Epstein-Barr virus nuclear antigen 2 in lymphoblastoid cell lines.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways.BMC structural biology · 2006Article
- The perichromosomal layer.Chromosoma · 2005Review
- Mpe1, a zinc knuckle protein, is an essential component of yeast cleavage and polyadenylation factor required for the cleavage and polyadenylation of mRNA.Molecular and cellular biology · 2001Article
- Yeast and human genes that affect the Escherichia coli SOS response.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Terminal differentiation is associated with repression in the expression of the proliferation potential proteins (P2P) subset of heterogeneous nuclear ribonucleoprotein (hnRNP) proteins. We report here the cloning and characterization of a 5173-bp P2P-related (P2P-R) cDNA that contains a 4214-bp open reading frame. Probes to this cDNA detect a single 8-kb mRNA in multiple murine tissues and in proliferating 3T3T cells, but not in terminally differentiated 3T3T adipocytes. Evidence that this cDNA can encode peptides with domains for hnRNP association was established by showing that such peptides are recognized by two monoclonal antibodies known to detect core hnRNP proteins, and by showing that the C130 monoclonal antibody, produced against a cDNA-derived fusion protein, also selectively detects native P2P hnRNP proteins. In addition, P2P-R cDNA-derived fusion proteins bind single-stranded nucleic acids, and a P2P-R cDNA-derived antisense oligonucleotide selectively represses P2P expression. Because terminal differentiation is associated with modulation in Rb1 function, we assayed if products of this cDNA might interact with Rb1. Evidence that the P2P-R cDNA encodes a protein domain that binds Rb1 was established using a glutathione S-transferase fusion protein to selectively precipitate Rb1 from cellular extracts. Data also show that this binding is reduced by competition with the adenovirus E1a protein, indicating that binding occurs through the "pocket" domain of Rb1. These results establish that the P2P-R cDNA encodes protein domains involved in both hnRNP association and Rb1 binding and complement recent reports that localize Rb1 to sites of RNA processing in the nucleus.
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