Signal Transduction from the Cytoplasm to the Cell Nucleus by NF-κB/Rel Transcription Factors

1995 ◽  
pp. 279-303 ◽  
Author(s):  
M. Lienhard Schmitz ◽  
Patrick A. Baeuerle
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Cell Nucleus

scholarly journals Divergence in Coding Sequence and Expression of Different Functional Categories of Immune Genes between Two Wild Rodent Species

2021 ◽  
Vol 13 (3) ◽  
Author(s):  
Xiuqin Zhong ◽  
Max Lundberg ◽  
Lars Råberg
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Immune Function ◽  
Sequence Divergence ◽  
Expression Divergence ◽  
Functional Categories ◽  
Coding Sequence ◽  
Immune Genes ◽  
Genes Encoding ◽  
Signal Transduction Proteins

Abstract Differences in immune function between species could be a result of interspecific divergence in coding sequence and/or expression of immune genes. Here, we investigate how the degree of divergence in coding sequence and expression differs between functional categories of immune genes, and if differences between categories occur independently of other factors (expression level, pleiotropy). To this end, we compared spleen transcriptomes of wild-caught yellow-necked mice and bank voles. Immune genes expressed in the spleen were divided into four categories depending on the function of the encoded protein: pattern recognition receptors (PRR); signal transduction proteins; transcription factors; and cyto- and chemokines and their receptors. Genes encoding PRR and cyto-/chemokines had higher sequence divergence than genes encoding signal transduction proteins and transcription factors, even when controlling for potentially confounding factors. Genes encoding PRR also had higher expression divergence than genes encoding signal transduction proteins and transcription factors. There was a positive correlation between expression divergence and coding sequence divergence, in particular for PRR genes. We propose that this is a result of that divergence in PRR coding sequence leads to divergence in PRR expression through positive feedback of PRR ligand binding on PRR expression. When controlling for sequence divergence, expression divergence of PRR genes did not differ from other categories. Taken together, the results indicate that coding sequence divergence of PRR genes is a major cause of differences in immune function between species.

scholarly journals Identification and Characterization of Genes Required for Cell-to-Cell Fusion in Neurospora crassa

2011 ◽  
Vol 10 (8) ◽  
pp. 1100-1109 ◽  
Author(s):  
Ci Fu ◽  
Priyadarshini Iyer ◽  
Amrita Herkal ◽  
Julia Abdullah ◽  
Angela Stout ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Neurospora Crassa ◽  
Cell Fusion ◽  
Single Gene ◽  
Vesicular Trafficking ◽  
Screening Procedure ◽  
Fusion Genes ◽  
Fusion Event ◽  
Screening Experiments

ABSTRACT A screening procedure was used to identify cell fusion (hyphal anastomosis) mutants in the Neurospora crassa single gene deletion library. Mutants with alterations in 24 cell fusion genes required for cell fusion between conidial anastomosis tubes (CATs) were identified and characterized. The cell fusion genes identified included 14 genes that are likely to function in signal transduction pathways needed for cell fusion to occur ( mik-1 , mek-1 , mak-1 , nrc-1 , mek-2 , mak-2 , rac-1 , pp2A , so/ham-1 , ham-2 , ham-3 , ham-5 , ham-9 , and mob3 ). The screening experiments also identified four transcription factors that are required for cell fusion ( adv-1 , ada-3 , rco-1 , and snf5 ). Three genes encoding proteins likely to be involved in the process of vesicular trafficking were also identified as needed for cell fusion during the screening ( amph-1 , ham-10 , pkr1 ). Three of the genes identified by the screening procedure, ham-6 , ham-7 , and ham-8 , encode proteins that might function in mediating the plasma membrane fusion event. Three of the putative signal transduction proteins, three of the transcription factors, the three putative vesicular trafficking proteins, and the three proteins that might function in mediating cell fusion had not been identified previously as required for cell fusion.

scholarly journals The molecular mechanisms of multidrug resistance of human glioblastomas

2021 ◽  
Vol 67 (1) ◽  
pp. 20-28
Author(s):  
Alexandr Chernov ◽  
Irina Baldueva ◽  
Tatyana Nekhaeva ◽  
Elvira Galimova ◽  
Diana Alaverdian ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Drug Resistance ◽  
Transcription Factors ◽  
Growth Factors ◽  
Multidrug Resistance ◽  
Tumor Suppressor Genes ◽  
Molecular Mechanisms ◽  
Molecular Targets ◽  
Polymorphic Variants ◽  
Signal Transduction Proteins

In review discusses the phenomenon of drug resistance of GB in the context of the expression of ABC family transporter proteins and the processes of proliferation, angiogenesis, recurrence and death. The emphasis is on the identifying for molecular targets among growth factors, receptors, signal transduction proteins, microRNAs, transcription factors, proto-oncogenes, tumor suppressor genes and their polymorphic variants (SNPs) for the development and creation of targeted anticancer drugs.

scholarly journals Epidermal growth factor and Ras regulate gene expression in GH4 pituitary cells by separate, antagonistic signal transduction pathways.

1995 ◽  
Vol 15 (12) ◽  
pp. 6777-6784 ◽  
Author(s):  
C A Pickett ◽  
A Gutierrez-Hartmann
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Growth Factor ◽  
Map Kinase ◽  
Dominant Negative ◽  
Neuroendocrine Cells ◽  
Dependent Manner ◽  
Epidermal Growth ◽  
Dose Dependent

We have previously demonstrated that epidermal growth factor (EGF) produces activation of the rat prolactin (rPRL) promoter in GH4 neuroendocrine cells via a Ras-independent mechanism. This Ras independence of the EGF response appears to be cell rather than promoter specific. Oncogenic Ras also produces activation of the rPRL promoter when transfected into GH4 cells and requires the sequential activation of Raf kinase, mitogen-activated protein (MAP) kinase, and c-Ets-1/GHF-1 to mediate this response. In these studies, we have investigated the interaction between EGF and Ras in stimulating rPRL promoter activity and the role of Raf and MAP kinases in mediating the EGF response. We have also examined the role of several transcription factors and used various promoter mutants of the rPRL gene in order to better define the trans- and cis-acting components of the EGF response. EGF treatment of GH4 cells inhibits activation of the rPRL promoter produced by transfection of V12Ras from 24- to 4-fold in an EGF dose-dependent manner. This antagonistic effect of EGF and Ras is mutual in that transfection of V12Ras also blocks EGF-induced activation of the rPRL promoter in a Ras dose-dependent manner, from 5.5- to 1.6-fold. Transfection of a plasmid encoding the dominant-negative Raf C4 blocks Ras-induced activation by 66% but fails to inhibit EGF-mediated activation of the rPRL promoter. Similarly, transfection of a construct encoding an inhibitory form of MAP kinase decreases the Ras response by 50% but does not inhibit the EGF response. Previous studies have demonstrated that c-Ets-1 is necessary and that GHF-1 acts synergistically with c-Ets-1 in the Ras response of the rPRL promoter. In contrast, overexpression of neither c-Ets-1 nor GHF-1 enhanced EGF-mediated activation of the rPRL promoter, and dominant-negative forms of these transcription factors failed to inhibit the EGF response. Using 5' deletion and site-specific mutations, we have mapped the EGF response to two regions on the proximal rPRL promoter. One region maps between -255 and -212, near the Ras response element, and a second maps between -125 and -54. The latter region appears to involve footprint 2, a previously identified repressor site on the rPRL promoter. Neither footprint 1 nor 3, known GHF-1 binding sites, appears to be crucial to RGF-mediated rPRL promoter activation. The results of these studies indicate that in GH4 neuroendocrine cells, rPRL gene regulation by EGF is mediated by a signal transduction pathway that is separate and antagonistic to the Ras pathway. Hence, the functional role of the Ras/Raf/MAP kinase pathway in mediating transcriptional responses to EGF and other receptor tyrosine kinase may differ in highly specialized cell types.

scholarly journals Beyond microarrays: Finding key transcription factors controlling signal transduction pathways

2006 ◽  
Vol 7 (S2) ◽  
Author(s):  
Alexdander Kel ◽  
Nico Voss ◽  
Ruy Jauregui ◽  
Olga Kel-Margoulis ◽  
Edgar Wingender
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Signal Transduction Pathways

scholarly journals Brassinosteroid signal transduction from cell-surface receptor kinases to nuclear transcription factors

2009 ◽  
Vol 11 (10) ◽  
pp. 1254-1260 ◽  
Author(s):  
Tae-Wuk Kim ◽  
Shenheng Guan ◽  
Yu Sun ◽  
Zhiping Deng ◽  
Wenqiang Tang ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Transcription Factors ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Receptor Kinases ◽  
Surface Receptor

scholarly journals A mini-review of TAT-MyoD fused proteins: state of the art and problems to solve

2017 ◽  
Vol 27 (4) ◽  
Author(s):  
Marco Patruno ◽  
Luca Melotti ◽  
Chiara Gomiero ◽  
Roberta Sacchetto ◽  
Ohad Topel ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Viral Replication ◽  
Cell Nucleus ◽  
State Of The Art ◽  
Transcriptional Activator ◽  
Short Review ◽  
Tat Protein ◽  
Small Peptide ◽  
Extracellular Milieu ◽  
Innovative Methodology

The transcriptional activator TAT is a small peptide essential for viral replication and possesses the property of entering the cells from the extracellular milieu, acting as a membrane shuttle. In order to safely differentiate cells an innovative methodology, based on the fusion of transcription factors and the TAT sequence, is discussed in this short review. In several studies, it has been demonstrated that TAT protein can be observed in the cell nucleus after few hours from the inoculation although its way of action is not fully understood. However, further studies will be necessary to develop this methodology for clinical purposes.

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