NDLI: Biological function of the retinoblastoma protein requires distinct domains for hyperphosphorylation and transcription factor binding.

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Transcription enhances intrachromosomal homologous recombination in mammalian cells.

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Multiple in vivo footprints are specific to the active allele of the X-linked human hypoxanthine phosphoribosyltransferase gene 5' region: implications for X chromosome inactivation.

Mitogenic signaling by colony-stimulating factor 1 and ras is suppressed by the ets-2 DNA-binding domain and restored by myc overexpression.

Biological function of the retinoblastoma protein requires distinct domains for hyperphosphorylation and transcription factor binding.

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Effect of terminal nonhomologies on homologous recombination in Xenopus laevis oocytes.

p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain.

A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation.

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Multiple functional domains of human U2 small nuclear RNA: strengthening conserved stem I can block splicing.

Fission yeast pap1-dependent transcription is negatively regulated by an essential nuclear protein, crm1.

Biochemical and cytological changes associated with expression of deregulated pp60src in Xenopus oocytes.

Unstable amplification of two extrachromosomal elements in alpha-difluoromethylornithine-resistant Leishmania donovani.

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A mammalian cell line deficient in activity of the DNA repair enzyme 5-hydroxymethyluracil-DNA glycosylase is resistant to the toxic effects of the thymidine analog 5-hydroxymethyl-2'-deoxyuridine.

Osteoblast-specific expression of growth hormone stimulates bone growth in transgenic mice.

Association of Src-like protein tyrosine kinases with the CD2 cell surface molecule in rat T lymphocytes and natural killer cells.

Relative roles of signals upstream of AAUAAA and promoter proximity in regulation of human immunodeficiency virus type 1 mRNA 3' end formation.

Isolation and structural analysis of a 1.2-megabase N-myc amplicon from a human neuroblastoma.

The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine phosphatases that negatively regulate mitosis.

Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding.

Alternative topogenic signals in peroxisomal citrate synthase of Saccharomyces cerevisiae.

Identification of a cysteine-rich receptor for fibroblast growth factors.

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Novel member of the zinc finger superfamily: A C2-HC finger that recognizes a glia-specific gene.

Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae.

Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nuclei.

Repression and activation of the Drosophila dopa decarboxylase gene in glia.

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Sequence of cDNA comprising the human pur gene and sequence-specific single-stranded-DNA-binding properties of the encoded protein.

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Truncated protein phosphatase GLC7 restores translational activation of GCN4 expression in yeast mutants defective for the eIF-2 alpha kinase GCN2.

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

Evidence that POB1, a Saccharomyces cerevisiae protein that binds to DNA polymerase alpha, acts in DNA metabolism in vivo.

CTF4 (CHL15) mutants exhibit defective DNA metabolism in the yeast Saccharomyces cerevisiae.

Two cellular proteins bind specifically to a purine-rich sequence necessary for the destabilization function of a c-fos protein-coding region determinant of mRNA instability.

A mutation outside the two zinc fingers of ADR1 can suppress defects in either finger.

P25 gene regulation in Bombyx mori silk gland: two promoter-binding factors have distinct tissue and developmental specificities.

A mutation in the tRNA nucleotidyltransferase gene promotes stabilization of mRNAs in Saccharomyces cerevisiae.

The polyomavirus enhancer activates chromatin accessibility on integration into the HPRT gene.

Multiple mechanisms of interference between transformation and differentiation in thyroid cells.

Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases.

Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP.

The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.

The SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels.

The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment.

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Biological function of the retinoblastoma protein requires distinct domains for hyperphosphorylation and transcription factor binding.

Content Provider	PubMed Central
Author	Qian, Y. Luckey, C. Horton, L. Esser, M. Templeton, D. J.
Abstract	Despite the importance of the retinoblastoma susceptibility gene to tumor growth control, the structural features of its encoded protein (pRb) and their relationship to protein function have not been well explored. We constructed a panel of deletion mutants of pRb expression vectors and used a biological assay for pRb that measures growth inhibition and morphologic changes in pRb-transfected Saos-2 cells to correlate structural alterations of the pRb coding region with function. We tested the deleted proteins for the ability to bind to viral oncoprotein E1A and to the transcription factor E2F. We also measured the ability of the mutant proteins to become hyperphosphorylated in vivo and to be recognized as substrates in vitro by a cell cycle-regulatory kinase associated with cyclin A. We identified two regions of pRb that are required for E2F binding and for hyperphosphorylation. E1A binding domains partially overlap but are distinct from both of these other two regions. Biological function of pRb is dependent on retention of the integrity of both of these biochemically defined domains. These data support the model that pRb is a transducer of afferent signals (via the kinase that phosphorylates it) and efferent signals (through transcription factor binding), using distinct structural elements. Preservation of both of these features is essential for the ability of pRb to induce growth inhibition and morphologic changes upon reintroduction into transfected cells.
Starting Page	5363
File Format	PDF
ISSN	10985549
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	12
Volume Number	12
Language	English
Publisher Date	1992-12-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

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