scholarly journals Characterization of a Myeloid Tyrosine Phosphatase, Lyp, and Its Role in the Bcr-Abl Signal Transduction Pathway

2003 ◽  
Vol 278 (30) ◽  
pp. 27413-27420 ◽  
Author(s):  
Wenwen Chien ◽  
Nicola Tidow ◽  
Elizabeth A. Williamson ◽  
Lee-Yung Shih ◽  
Utz Krug ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Tyrosine Phosphatase ◽  
Signal Transduction Pathway ◽  
Transduction Pathway

Abstract 741: Characterization of high-grade serous ovarian carcinoma by measuring functional signal transduction pathway activity

2021 ◽  
Author(s):  
Phyllis van der Ploeg ◽  
Laura van Lieshout ◽  
Yvonne Wesseling-Rozendaal ◽  
Anja van de Stolpe ◽  
Diederick Keizer ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Ovarian Carcinoma ◽  
Signal Transduction Pathway ◽  
High Grade ◽  
Transduction Pathway ◽  
Pathway Activity ◽  
Serous Ovarian Carcinoma

scholarly journals Genetic evidence for signal transduction within the Bacillus subtilis GerA germinant receptor

2021 ◽  
Author(s):  
Jeremy D. Amon ◽  
Lior Artzi ◽  
David Z. Rudner
Keyword(s):  
Signal Transduction ◽  
Bacillus Subtilis ◽  
Signal Transduction Pathway ◽  
Dominant Negative ◽  
Transduction Pathway ◽  
Sense And Respond ◽  
Enrichment Strategy ◽  
Functional Receptor

Bacterial spores can rapidly exit dormancy through the process of germination. This process begins with the activation of nutrient receptors embedded in the spore membrane. The prototypical germinant receptor in Bacillus subtilis responds to L-alanine and is thought to be a complex of proteins encoded by the genes in the gerA operon: gerAA , gerAB , and gerAC . The GerAB subunit has recently been shown to function as the nutrient sensor, but beyond contributing to complex stability, no additional functions have been attributed to the other two subunits. Here, we investigate the role of GerAA. We resurrect a previously characterized allele of gerA (termed gerA* ) that carries a mutation in gerAA and show it constitutively activates germination even in the presence of a wild-type copy of gerA . Using an enrichment strategy to screen for suppressors of gerA* , we identified mutations in all three gerA genes that restore a functional receptor. Characterization of two distinct gerAB suppressors revealed that one ( gerAB[E105K]) reduces the GerA complex's ability to respond to L-alanine, while another ( gerAB[F259S] ) disrupts the germinant signal downstream of L-alanine recognition. These data argue against models in which GerAA is directly or indirectly involved in germinant sensing. Rather, our data suggest that GerAA is responsible for transducing the nutrient signal sensed by GerAB. While the steps downstream of gerAA have yet to be uncovered, these results validate the use of a dominant-negative genetic approach in elucidating the gerA signal transduction pathway. Importance Endospore formers are a broad group of bacteria that can enter dormancy upon starvation and exit dormancy upon sensing the return of nutrients. How dormant spores sense and respond to these nutrients is poorly understood. Here, we identify a key step in the signal transduction pathway that is activated after spores detect the amino acid L-alanine. We present a model that provides a more complete picture of this process that is critical for allowing dormant spores to germinate and resume growth.

Characterization of the ABA signal transduction pathway in Vitis vinifera

Plant Science ◽  
2012 ◽  
Vol 187 ◽  
pp. 89-96 ◽  
Author(s):  
Uri Boneh ◽  
Iris Biton ◽  
Amnon Schwartz ◽  
Giora Ben-Ari
Keyword(s):  
Signal Transduction ◽  
Vitis Vinifera ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Aba Signal Transduction

scholarly journals A Genetic Analysis of Glucocorticoid Receptor Signaling: Identification and Characterization of Ligand-Effect Modulators in Saccharomyces cerevisiae

Genetics ◽  
2000 ◽  
Vol 156 (3) ◽  
pp. 963-972
Author(s):  
Raquel Sitcheran ◽  
Roger Emter ◽  
Anastasia Kralli ◽  
Keith R Yamamoto
Keyword(s):  
Signal Transduction ◽  
Glucocorticoid Receptor ◽  
Cellular Response ◽  
Transmembrane Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Ligand Effect ◽  
Yeast Genetic ◽  
Identification And Characterization

Abstract To find novel components in the glucocorticoid signal transduction pathway, we performed a yeast genetic screen to identify ligand-effect modulators (LEMs), proteins that modulate the cellular response to hormone. We isolated several mutants that conferred increased glucocorticoid receptor (GR) activity in response to dexamethasone and analyzed two of them in detail. These studies identify two genes, LEM3 and LEM4, which correspond to YNL323w and ERG6, respectively. LEM3 is a putative transmembrane protein of unknown function, and ERG6 is a methyltransferase in the ergosterol biosynthetic pathway. Analysis of null mutants indicates that LEM3 and ERG6 act at different steps in the GR signal transduction pathway.

scholarly journals Characterization of phosphoinositide-specific phospholipase C in rat colonocyte membranes

1993 ◽  
Vol 292 (1) ◽  
pp. 271-276 ◽  
Author(s):  
M J G Bolt ◽  
B M Bissonnette ◽  
R K Wali ◽  
S C Hartmann ◽  
T A Brasitus ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Monoclonal Antibodies ◽  
Phospholipase C ◽  
Plasma Membranes ◽  
Signal Transduction Pathway ◽  
Protein S ◽  
Transduction Pathway ◽  
Intestinal Physiology ◽  
Key Enzyme

The phosphoinositide signal transduction pathway mediates important processes in intestinal physiology, yet the key enzyme, phosphoinositide-specific phospholipase C (PI-PLC), is not well-characterized in the colon. PI-PLC activity was examined in rat colonic membranes using exogenous [3H]phosphatidylinositol 4,5-bisphosphate (PIP2) as substrate, and beta-glycerophosphate to suppress degradation of substrate or product. The activity of membrane PI-PLC increased 6-fold with the addition of alamethicin, and a further 2-3-fold enhancement was observed with 10 microM guanosine 5′-[gamma-thio]triphosphate (GTP[S]), suggesting the involvement of G-protein(s). The effect of GTP[S] appeared to be specific, as up to 100 microM adenosine 5′-[gamma-thio]-triphosphate failed to stimulate PI-PLC activity, and guanosine 5′-[beta-thio]diphosphate inhibited activity. The response of membrane PI-PLC to Ca2+ was biphasic, while > 0.5 mM Mg2+ was inhibitory with or without GTP[S]. Comparable total PI-PLC activities and responses to GTP[S] and Ca2+ were observed in purified brush-border and basolateral membranes. Western immunoblots probed with monoclonal antibodies to PLC isoenzymes PLC-beta 1, -gamma 1 and -delta 1 demonstrated that these antipodal plasma membranes contain predominantly the PLC-delta 1 isoform, with small amounts of PLC-gamma 1 present but no detectable PLC-beta 1. PLC-gamma 1 was the major isoform detected in cytosol.

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