Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product

Defeo-Jones, Deborah; Huang, Pearl S.; Jones, Raymond E.; Haskell, Kathleen; Vuocolo, G A; Hanobik, Michelle G.; Huber, Hans E.; Oliff, A

doi:10.1038/352251a0

Cited by 322 publications

(212 citation statements)

References 23 publications

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“…It is ubiquitously expressed in adult tissues and has jmjN, jmjC, PHD, and ARID sequences. Among the over 100 pRB binding proteins, RBP1 and RBP2 were identified as the first cellular pRB binding proteins (Defeo-Jones et al, 1991). Although the function has remained unknown for a long time, roles in cell differentiation were recently proposed (Benevolenskaya et al, 2005).…”

Section: Rbp2mentioning

confidence: 99%

Roles of jumonji and jumonji family genes in chromatin regulation and development

Takeuchi

Watanabe

Takano-Shimizu

et al. 2006

Developmental Dynamics

176

148

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The jumonji (jmj) gene was identified by a mouse gene trap approach and has essential roles in the development of multiple tissues. The Jmj protein has a DNA binding domain, ARID, and two conserved jmj domains (jmjN and jmjC). In many diverse species including bacteria, fungi, plants, and animals, there are many jumonji family proteins that have only the jmjC domain or both jmj domains. Recently, Jmj protein was found to be a transcriptional repressor. Several proteins in the jumonji family are involved in transcriptional repression and/or chromatin regulation. Most recently, one of the human members has been shown to be a histone demethylase, and the jmjC domain is essential for the demethylase activity. Meanwhile, more and more evidence indicating that the jumonji family proteins play important roles during development is accumulating. Many proteins in the jumonji family may regulate chromatin and gene expression, and control development through various signaling pathways. Here, we highlight the roles of jmj and jumonji family proteins in chromatin regulation and development. Developmental Dynamics 235: 2449 -2459, 2006.

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Section: Rbp2mentioning

confidence: 99%

Roles of jumonji and jumonji family genes in chromatin regulation and development

Takeuchi

Watanabe

Takano-Shimizu

et al. 2006

Developmental Dynamics

176

148

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“…Since RBP-2 was previously suggested to be involved in pRb-phosphorylation control by direct protein-protein interaction, 4 we addressed the question whether RBP2-H1, the closest homolog of RBP-2, could also bind to pRb. While RBP2-H1 lacks the typical Leu-X-Cys-X-Glu-motif of some pRb-interacting proteins, it bears a homolog-domain of the non-T/E1A-pRb-binding domain of RBP-2.…”

Section: Rbp2-h1 Co-precipitates With Prbmentioning

confidence: 99%

“…Both proteins contain highly conserved pRb-binding motifs, which show a striking homology with viral oncogenic proteins such as E7, large T and E1A. 4 More recently, based on RNA-fingerprinting, we have described a novel homolog of RBP-2, termed RBP2-homolog 1 (RBP2-H1, NCBI Genebank Accession No. AF087481).…”

mentioning

confidence: 99%

Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas

et al. 2005

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In malignant melanomas, the loss of cell cycle control is thought to be due to a lack of retinoblastoma protein (pRb)-activity. Members of the previously described family of retinoblastoma-binding proteins (RBPs) are supposed to act as pRb-modulating factors. Based on RNA-fingerprinting of normal human melanocytes, we previously described a new family member with high sequence homology to the retinoblastoma-binding protein-2 (RBP-2), termed RBP2-Homolog 1 (RBP2-H1). Based on its UVB responsiveness, it was hypothesized that this gene may also play a role in melanocytic tumors. In the present study, we can confirm by real-time RT-PCR (six common melanocytic nevi, five advanced nodular melanomas and seven melanoma metastases) and immunohistochemistry (tissue microarrays: 52 melanocytic nevi, 60 melanomas, 60 metastases; and conventional sections: five common nevi, four advanced nodular melanomas, five melanoma metastases) that RBP2-H1 expression is progressively downregulated in advanced and metastatic melanomas in vivo with a certain intratumoral heterogeneity. Whereas benign melanocytic nevi are RBP2-H1 positive in about 70% of the cases, a lack of RBP2-H1 expression was found in 90% of the primary malignant melanomas and 70% of the melanoma metastases, respectively. Interestingly, a similar deficiency can be found in glioblastomas, but not epithelial cancers. In accordance to the in vivo data, established melanoma cell lines exhibit low but heterogeneous levels of RBP2-H1 expression. By co-immunoprecipitation, we provide the first evidence that a subfraction of total RBP2-H1 can bind to pRb, which makes this protein a true pRb-interacting factor. We conclude that loss of RBP2-H1 is a common finding in the progression of malignant melanomas. Since a direct interaction of RBP2-H1 and pRb seems possible, the loss of RBP2-H1 may possibly contribute to uncontrolled growth in malignant melanomas.

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“…Histone demethylases have been linked to tumor formation; JARID1A was originally identified from its interaction with retinoblastomaassociated protein 1, a tumor suppressor protein. 8 Small molecule inhibitors of both histone methyl transferases and demethylases are now being sought. 19 In this way the balance between the activity of methylating and demethylating enzymes can be manipulated to control gene expression with the possibility of tilting expression levels away from a disease phenotype.…”

Section: Resultsmentioning

confidence: 99%

“…8 It has the JmjN and JmjC domains, the JmjC domain is predicted to be a metalloenzyme catalytic motif that is required for demethylase activity. Other conserved motifs include an ARID domain involved in binding A/T rich DNA, a single C5HC2 zinc-finger, and three PHD fingers involved in mediating protein-protein interactions and binding methylated-lysine residues.…”

Section: Introductionmentioning

confidence: 99%

The histone demethylase JARID1A is associated with susceptibility to ankylosing spondylitis

et al. 2011

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Associations with disease identified by genome-wide association studies (GWAS) must be replicated and refined to validate causative variants. In the Wellcome Trust Case Control Consortium (WTCCC) GWAS using 14 500 non-synonymous single nucleotide polymorphisms (nsSNP), rs11062385 (a nsSNP in JARID1A) showed nominal association with ankylosing spondylitis (AS) (P ¼ 0.0006, odds ratio (OR) ¼ 1.26, 95% confidence interval (95% CI) ¼ 1.1-1.4). To replicate and refine the association of JARID1A, rs11062385 was genotyped in 730 further cases and compared with allele frequencies in non-AS disease cohorts typed by WTCCC. We replicated the initial association (P ¼ 0.04, OR ¼ 1.16, 95% CI ¼ 1.01-1.34) and identified a strengthened association with AS in a meta-analysis of this new study combined with the original WTCCC study (P ¼ 0.0001, OR ¼ 1.21, 95% CI ¼ 1.10-1.33). We also genotyped nine further intronic tagging SNPs in JARID1A in 1604 AS cases and 1020 new control samples, but none was associated with AS. JARID1A or a locus in strong linkage disequilibrium with it is a positional candidate for susceptibility to AS.

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Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product

Cited by 322 publications

References 23 publications

Roles of jumonji and jumonji family genes in chromatin regulation and development

Roles of jumonji and jumonji family genes in chromatin regulation and development

Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas

The histone demethylase JARID1A is associated with susceptibility to ankylosing spondylitis

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