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Results: 321 to 329 of 329

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An E2F dominant negative mutant blocks E1A induced cell cycle progression.
Dobrowolski SF, Stacey DW, Harter ML, Stine JT, Hiebert SW
(1994) Oncogene 9: 2605-12
MeSH Terms: 3T3 Cells, Adenovirus E1A Proteins, Animals, Carrier Proteins, Cell Cycle, Cell Cycle Proteins, DNA, DNA-Binding Proteins, E2F Transcription Factors, E2F1 Transcription Factor, Genes, myc, Glutathione Transferase, HeLa Cells, Humans, Mice, Mutation, Retinoblastoma-Binding Protein 1, Transcription Factor DP1, Transcription Factors
Show Abstract · Added June 10, 2010
E2F is a cellular transcription factor that is regulated during the cell cycle through interactions with the product of the retinoblastoma susceptibility gene (RB1) and the pRb-like p107 and p130 proteins. Analysis of mutations within both adenovirus E1A and pRb, which affected their ability to regulate cellular proliferation and alter E2F activity, suggested that E2F may play a role in cell cycle progression. Microinjection of a GST-E2F-1 fusion protein into quiescent Balb/c 3T3 cells induced DNA synthesis whereas co-injection of GST-E2F-1 and GST-E2F(95-191) protein, encoding only the DNA binding domain of E2F-1, blocked the induction of S-phase. While E1A likely targets multiple cellular pathways, co-injection of the GST-E2F(95-191) dominant inhibitory protein with 12S E1A protein blocked E1A-mediated induction of DNA synthesis, suggesting that the E2F-dependent pathway is dominant. Analysis of the interval required for microinjected quiescent cells to enter S-phase indicated that E2F-1 acted faster than either E1A or serum.
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19 MeSH Terms
E2F-independent transcriptional repression by p107, a member of the retinoblastoma family of proteins.
Dagnino L, Zhu L, Skorecki KL, Moses HL
(1995) Cell Growth Differ 6: 191-8
MeSH Terms: Carrier Proteins, Cell Cycle Proteins, DNA-Binding Proteins, E2F Transcription Factors, Genes, Retinoblastoma, Genes, myc, HeLa Cells, Humans, Multigene Family, Nuclear Proteins, Promoter Regions, Genetic, Repressor Proteins, Retinoblastoma-Binding Protein 1, Retinoblastoma-Like Protein p107, TATA Box, Transcription Factor DP1, Transcription Factors, Tumor Cells, Cultured, Viral Proteins
Show Abstract · Added February 17, 2014
The Rb family of proteins includes pRb, p107, and p130. These nuclear polypeptides associate with cyclins and transcription factors involved in the control of cell proliferation. This has suggested that members of the pRb family may modulate cell growth, at least in part, by regulating gene transcription. We have investigated the ability of p107 to modulate transcription and compared it with that of pRb. Whereas pRb inhibition of the c-myc promoter required the presence of E2F sites, p107 inhibition did not. Moreover, p107, but not pRb, repressed transcription from other promoters including fibronectin, herpes virus thymidine kinase, and a synthetic promoter containing a SV40 repeat activator motif upstream from the adenovirus major late-promoter TATA box. In contrast, the activity of the TATA-lacking promoters from the epidermal growth factor receptor and the cytoplasmic phospholipase A2 genes was unaffected by either p107 or pRb. Likewise, overexpression of p107 or pRb had no effect on the activity of a synthetic promoter lacking a TATA box and containing the SV40 repeat motif upstream from the terminal transferase gene initiator element. The domains in p107 required for transcriptional repression included the A segment of the pocket region and parts of the B segment, but not the spacer domain. In spite of their structural similarities, p107 and pRb may contribute to the control of cell proliferation by modulating the transcription of different genes.
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19 MeSH Terms
The Wee1 protein kinase regulates T14 phosphorylation of fission yeast Cdc2.
Den Haese GJ, Walworth N, Carr AM, Gould KL
(1995) Mol Biol Cell 6: 371-85
MeSH Terms: Base Sequence, Cell Cycle Proteins, Checkpoint Kinase 1, G2 Phase, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Fungal, Genes, Fungal, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Proteins, Phosphoprotein Phosphatases, Phosphorylation, Protein Kinases, Protein-Tyrosine Kinases, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Threonine, Tyrosine, cdc25 Phosphatases
Show Abstract · Added March 5, 2014
The Cdc2 protein kinase is a key regulator of the G1-S and G2-M cell cycle transitions in the fission yeast Schizosaccharomyces pombe. The activation of Cdc2 at the G2-M transition is triggered by dephosphorylation at a conserved tyrosine residue Y15. The level of Y15 phosphorylation is controlled by the Wee1 and Mik1 protein kinases acting in opposition to the Cdc25 protein phosphatase. Here, we demonstrate that Wee1 overexpression leads to a high stoichiometry of phosphorylation at a previously undetected site in S. pombe Cdc2, T14. T14 phosphorylation was also detected in certain cell cycle mutants blocked in progression through S phase, indicating that T14 phosphorylation might normally occur at low stoichiometry during DNA replication or early G2. Strains in which the chromosomal copy of cdc2 was replaced with either a T14A or a T14S mutant allele were generated and the phenotypes of these strains are consistent with T14 phosphorylation playing an inhibitory role in the activation of Cdc2 as it does in higher eukaryotes. We have also obtained evidence that Wee1 but not Mik1 or Chk1 is required for phosphorylation at this site, that the Mik1 and Chk1 protein kinases are unable to drive T14 phosphorylation in vivo, that residue 14 phosphorylation requires previous phosphorylation at Y15, and that the T14A mutant, unlike Y15F, is recessive to wild-type Cdc2 activity. Finally, the normal duration of G2 delay after irradiation or hydroxyurea treatment in a T14A mutant strain indicates that T14 phosphorylation is not required for the DNA damage or replication checkpoint controls.
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19 MeSH Terms
Schizosaccharomyces pombe cdc4+ gene encodes a novel EF-hand protein essential for cytokinesis.
McCollum D, Balasubramanian MK, Pelcher LE, Hemmingsen SM, Gould KL
(1995) J Cell Biol 130: 651-60
MeSH Terms: Amino Acid Sequence, Base Sequence, Cell Compartmentation, Cell Cycle Proteins, Cell Division, Cloning, Molecular, Cytoskeletal Proteins, Escherichia coli, F-Box Proteins, Fluorescent Antibody Technique, Fungal Proteins, Genes, Fungal, Molecular Sequence Data, Mutation, Phenotype, Precipitin Tests, Protein Binding, Recombinant Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Ubiquitin-Protein Ligases
Show Abstract · Added March 5, 2014
Schizosaccharomyces pombe cells divide by medial fission. One class of cell division mutants (cdc), the late septation mutants, defines four genes: cdc3, cdc4, cdc8, and cdc12 (Nurse, P., P. Thuriaux, and K. Nasmyth. 1976. Mol. & Gen. Genet. 146:167-178). We have cloned and characterized the cdc4 gene and show that the predicted gene product. Cdc4p, is a 141-amino acid polypeptide that is similar in sequence to EF-hand proteins including myosin light chains, calmodulin, and troponin C. Two temperature-sensitive lethal alleles, cdc4-8 and cdc4-31, accumulate multiple nuclei and multiple improper F-actin rings and septa but fail to complete cytokinesis. Deletion of cdc4 also results in a lethal terminal phenotype characterized by multinucleate, elongated cells that fail to complete cytokinesis. Sequence comparisons suggest that Cdc4p may be a member of a new class of EF-hand proteins. Cdc4p localizes to a ringlike structure in the medial region of cells undergoing cytokinesis. Thus, Cdc4p appears to be an essential component of the F-actin contractile ring. We find that Cdc4 protein forms a complex with a 200-kD protein which can be cross-linked to UTP, a property common to myosin heavy chains. Together these results suggest that Cdc4p may be a novel myosin light chain.
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23 MeSH Terms
The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.
Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ
(1995) Nat Struct Biol 2: 790-6
MeSH Terms: Amino Acid Sequence, Animals, Calcium-Binding Proteins, Cattle, Cell Cycle Proteins, Humans, Magnetic Resonance Spectroscopy, Models, Chemical, Molecular Sequence Data, Protein Conformation, Protein Folding, Rabbits, S100 Calcium Binding Protein A6, S100 Proteins, Sequence Homology, Amino Acid, Solutions
Show Abstract · Added December 10, 2013
The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins.
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16 MeSH Terms
E2F transcription factor is a target for the RB protein and the cyclin A protein.
Nevins JR, Chellappan SP, Mudryj M, Hiebert S, Devoto S, Horowitz J, Hunter T, Pines J
(1991) Cold Spring Harb Symp Quant Biol 56: 157-62
MeSH Terms: Adenovirus Early Proteins, Binding Sites, Carrier Proteins, Cell Cycle, Cell Cycle Proteins, Cell Line, Cyclins, DNA-Binding Proteins, E2F Transcription Factors, Humans, Oncogene Proteins, Viral, Phosphorylation, Retinoblastoma Protein, Retinoblastoma-Binding Protein 1, Transcription Factor DP1, Transcription Factors, Transcription, Genetic
Added June 10, 2010
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17 MeSH Terms
Cell cycle regulation of the E2F transcription factor involves an interaction with cyclin A.
Mudryj M, Devoto SH, Hiebert SW, Hunter T, Pines J, Nevins JR
(1991) Cell 65: 1243-53
MeSH Terms: Adenovirus Early Proteins, Animals, Carrier Proteins, Cell Cycle, Cell Cycle Proteins, Cell Line, Cyclins, DNA-Binding Proteins, E2F Transcription Factors, Macromolecular Substances, Mice, Oncogene Proteins, Viral, Protein Binding, Retinoblastoma-Binding Protein 1, Time Factors, Transcription Factor DP1, Transcription Factors
Show Abstract · Added June 10, 2010
We have examined E2F binding activity in extracts of synchronized NIH 3T3 cells. During the G0 to G1 transition, there is a marked increase in the level of active E2F. Subsequently, there are changes in the nature of E2F-containing complexes. A G1-specific complex increases in abundance, disappears, and is then replaced by another complex as S phase begins. Analysis of extracts of thymidine-blocked cells confirms that the complexes are cell cycle regulated. We also show that the cyclin A protein is a component of the S phase complex. Each complex can be dissociated by the adenovirus E1A 12S product, releasing free E2F. The release of E2F from the cyclin A complex coincides with the stimulation of an E2F-dependent promoter. We suggest that these interactions control the activity of E2F and that disruption of the complexes by E1A contributes to a loss of cellular proliferation control.
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17 MeSH Terms
The E2F transcription factor is a cellular target for the RB protein.
Chellappan SP, Hiebert S, Mudryj M, Horowitz JM, Nevins JR
(1991) Cell 65: 1053-61
MeSH Terms: Adenovirus Early Proteins, Carrier Proteins, Cell Cycle Proteins, Cyclins, DNA-Binding Proteins, E2F Transcription Factors, Gene Expression Regulation, Humans, In Vitro Techniques, Macromolecular Substances, Oncogene Proteins, Viral, Phosphoproteins, Retinoblastoma Protein, Retinoblastoma-Binding Protein 1, Transcription Factor DP1, Transcription Factors, Transcription, Genetic
Show Abstract · Added June 10, 2010
Although it is generally believed that the product of the retinoblastoma susceptibility gene (RB1) is an important regulator of cell proliferation, the biochemical mechanism for its action is unclear. We now show that the RB protein is found in a complex with the E2F transcription factor and that only the under phosphorylated form of RB is in the E2F complex. Moreover, the adenovirus E1A protein can dissociate the E2F-RB complex, dependent on E1A sequence also critical for E1A to bind to RB. These sequences are also critical for E1A to immortalize primary cell cultures and to transform in conjunction with other oncogenes. Taken together, these results suggest that the interaction of RB with E2F is an important event in the control of cellular proliferation and that the dissociation of the complex is part of the mechanism by which E1A inactivates RB function.
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17 MeSH Terms
Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase.
Gould KL, Moreno S, Tonks NK, Nurse P
(1990) Science 250: 1573-6
MeSH Terms: Cell Cycle Proteins, Cyclins, Enzyme Activation, Fungal Proteins, Humans, Mitosis, Mutation, Phosphoprotein Phosphatases, Phosphorylation, Phosphotyrosine, Protein Kinases, Protein Tyrosine Phosphatases, Schizosaccharomyces, Transformation, Genetic, Tyrosine, ras-GRF1
Show Abstract · Added March 5, 2014
The onset of M phase requires the activation of the pp34 protein kinase in all eukaryotes thus far examined. In Schizosaccharomyces pombe, pp34 is phosphorylated on Tyr15, and dephosphorylation of this residue regulates the initiation of mitosis. In this study, it is shown that dephosphorylation of Tyr15 triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo, and that activation of fission yeast pp34 does not require threonine dephosphorylation. The complementary DNA that encoded the tyrosine phosphatase replaced the mitotic activator p80cdc25, closely associating the cdc25(+)-activating pathway with tyrosine dephosphorylation of pp34.
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16 MeSH Terms