scholarly journals Molecular Interaction Map of the Mammalian Cell Cycle Control and DNA Repair Systems

1999 ◽  
Vol 10 (8) ◽  
pp. 2703-2734 ◽  
Author(s):  
Kurt W. Kohn
Keyword(s):  
Cell Cycle ◽  
Molecular Species ◽  
Regulatory Network ◽  
Cell Cycle Control ◽  
Gene Promoter ◽  
Multiprotein Complexes ◽  
Mammalian Cell Cycle ◽  
Pertinent Information ◽  
Interaction Map ◽  
And Function

Eventually to understand the integrated function of the cell cycle regulatory network, we must organize the known interactions in the form of a diagram, map, and/or database. A diagram convention was designed capable of unambiguous representation of networks containing multiprotein complexes, protein modifications, and enzymes that are substrates of other enzymes. To facilitate linkage to a database, each molecular species is symbolically represented only once in each diagram. Molecular species can be located on the map by means of indexed grid coordinates. Each interaction is referenced to an annotation list where pertinent information and references can be found. Parts of the network are grouped into functional subsystems. The map shows how multiprotein complexes could assemble and function at gene promoter sites and at sites of DNA damage. It also portrays the richness of connections between the p53-Mdm2 subsystem and other parts of the network.

scholarly journals Role of Ubiquitin Ligases and the Proteasome in Oncogenesis: Novel Targets for Anticancer Therapies

2013 ◽  
Vol 31 (9) ◽  
pp. 1231-1238 ◽  
Author(s):  
Lindsey N. Micel ◽  
John J. Tentler ◽  
Peter G. Smith ◽  
Gail S. Eckhardt
Keyword(s):  
Cell Cycle ◽  
Anticancer Agents ◽  
Cell Cycle Control ◽  
Ubiquitin Proteasome System ◽  
Cellular Regulation ◽  
Ubiquitin Chain ◽  
Key Enzyme ◽  
Ubiquitin Proteasome ◽  
Enzyme Families ◽  
And Function

The ubiquitin proteasome system (UPS) regulates the ubiquitination, and thus degradation and turnover, of many proteins vital to cellular regulation and function. The UPS comprises a sequential series of enzymatic processes using four key enzyme families: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-carrier proteins), E3 (ubiquitin-protein ligases), and E4 (ubiquitin chain assembly factors). Because the UPS is a crucial regulator of the cell cycle, and abnormal cell-cycle control can lead to oncogenesis, aberrancies within the UPS pathway can result in a malignant cellular phenotype and thus has become an attractive target for novel anticancer agents. This article will provide an overall review of the mechanics of the UPS, describe aberrancies leading to cancer, and give an overview of current drug therapies selectively targeting the UPS.

Abnormalities in Cell Cycle Control in Cancer and Their Clinical Implications

1998 ◽  
Vol 84 (4) ◽  
pp. 421-433 ◽  
Author(s):  
Alessandro Sgambato ◽  
Giovanna Flamini ◽  
Achille Cittadini ◽  
I. Bernard Weinstein
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
Cell Transformation ◽  
Cell Cycle Control ◽  
Genomic Stability ◽  
Clinical Implications ◽  
Mammalian Cell Cycle ◽  
Carcinogenic Process ◽  
Review Current

Recent studies indicate that the functions of several genes that control the cell cycle are altered during the carcinogenic process and that these changes perturb both cell proliferation and genomic stability, thus promoting cell transformation and enhancing the process of tumor progression. The purpose of this paper is to review current information on the role of cyclins and related genes in the control of the mammalian cell cycle, the types of abnormalities in these genes found in human tumors and the possible clinical implications of these findings.

Cell Cycle Control: Molecular Interaction Map

2006 ◽  
Author(s):  
Kurt W Kohn ◽  
Mirit I Aladjem ◽  
Stefania Pasa ◽  
Silvio Parodi ◽  
Yves Pommier
Keyword(s):  
Cell Cycle ◽  
Molecular Interaction ◽  
Cell Cycle Control ◽  
Interaction Map

scholarly journals Asbestos exposure predicts cell cycle control gene promoter methylation in pleural mesothelioma

2008 ◽  
Vol 29 (8) ◽  
pp. 1555-1559 ◽  
Author(s):  
B. C. Christensen ◽  
J. J. Godleski ◽  
C. J. Marsit ◽  
E. A. Houseman ◽  
C. Y. Lopez-Fagundo ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Promoter Methylation ◽  
Asbestos Exposure ◽  
Cell Cycle Control ◽  
Gene Promoter ◽  
Pleural Mesothelioma ◽  
Control Gene

scholarly journals Seek and Destroy: SCF Ubiquitin Ligases in Mammalian Cell Cycle Control

Cell Cycle ◽  
2002 ◽  
Vol 1 (4) ◽  
pp. 248-252 ◽  
Author(s):  
Charles Spruck ◽  
Heimo M. Strohmaier
Keyword(s):  
Cell Cycle ◽  
Mammalian Cell ◽  
Cell Cycle Control ◽  
Ubiquitin Ligases ◽  
Mammalian Cell Cycle

scholarly journals Cell Cycle Control by Nuclear Sequestration ofCDC20andCDH1mRNA in Plant Stem Cells

2017 ◽  
Author(s):  
Weibing Yang ◽  
Raymond Wightman ◽  
Elliot M. Meyerowitz
Keyword(s):  
Cell Cycle ◽  
Nuclear Localization ◽  
Cell Cycle Control ◽  
Protein Translation ◽  
Messenger Rnas ◽  
Protein Coding ◽  
Rna Molecules ◽  
Nuclear Envelope Breakdown ◽  
And Function ◽  
Necessary And Sufficient

AbstractIn eukaryotic cells, most RNA molecules are exported into the cytoplasm after being transcribed in the nucleus. Long noncoding RNAs (lncRNAs) have been found to reside and function primarily inside the nucleus, but nuclear localization of protein-coding messenger RNAs (mRNAs) has been considered rare in both animals and plants. Here we show that two mRNAs, transcribed from theCDC20andCCS52B(plant orthologue ofCDH1) genes, are specifically sequestered inside the nucleus during the cell cycle. CDC20 and CDH1 both function as coactivators of the anaphase-promoting complex or cyclosome (APC/C) E3 ligase to trigger cyclin B (C YCB) destruction. In theArabidopsis thalianashoot apical meristem (SAM), we findCDC20andCCS52Bare co-expressed withCYCBsin mitotic cells.CYCBtranscripts can be exported and translated, whereasCDC20andCCS52BmRNAs are strictly confined to the nucleus at prophase and the cognate proteins are not translated until the redistribution of the mRNAs to the cytoplasm after nuclear envelope breakdown (NEBD) at prometaphase. The 5’ untranslated region (UTR) is necessary and sufficient forCDC20mRNA nuclear localization as well as protein translation. Mitotic enrichment ofCDC20andCCS52Btranscripts enables the timely and rapid activation of APC/C, while their nuclear sequestration at prophase appears to protect cyclins from precocious degradation.

scholarly journals A cell cycle regulatory network controlling NF-κB subunit activity and function

2007 ◽  
Vol 26 (23) ◽  
pp. 4841-4855 ◽  
Author(s):  
Benjamin Barré ◽  
Neil D Perkins
Keyword(s):  
Cell Cycle ◽  
Regulatory Network ◽  
A Cell ◽  
And Function

scholarly journals Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex

2018 ◽  
Vol 115 (35) ◽  
pp. E8191-E8200 ◽  
Author(s):  
Alessandro A. Rizzo ◽  
Faye-Marie Vassel ◽  
Nimrat Chatterjee ◽  
Sanjay D’Souza ◽  
Yunfeng Li ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cell Cycle Control ◽  
Translesion Synthesis ◽  
Functional Assay ◽  
Binding Motifs ◽  
Dimer Interface ◽  
Dimerization Interface ◽  
And Function

The translesion synthesis (TLS) polymerases Polζ and Rev1 form a complex that enables replication of damaged DNA. The Rev7 subunit of Polζ, which is a multifaceted HORMA (Hop1, Rev7, Mad2) protein with roles in TLS, DNA repair, and cell-cycle control, facilitates assembly of this complex by binding Rev1 and the catalytic subunit of Polζ, Rev3. Rev7 interacts with Rev3 by a mechanism conserved among HORMA proteins, whereby an open-to-closed transition locks the ligand underneath the “safety belt” loop. Dimerization of HORMA proteins promotes binding and release of this ligand, as exemplified by the Rev7 homolog, Mad2. Here, we investigate the dimerization of Rev7 when bound to the two Rev7-binding motifs (RBMs) in Rev3 by combining in vitro analyses of Rev7 structure and interactions with a functional assay in a Rev7−/−cell line. We demonstrate that Rev7 uses the conventional HORMA dimerization interface both to form a homodimer when tethered by the two RBMs in Rev3 and to heterodimerize with other HORMA domains, Mad2 and p31comet. Structurally, the Rev7 dimer can bind only one copy of Rev1, revealing an unexpected Rev1/Polζ architecture. In cells, mutation of the Rev7 dimer interface increases sensitivity to DNA damage. These results provide insights into the structure of the Rev1/Polζ TLS assembly and highlight the function of Rev7 homo- and heterodimerization.

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