scholarly journals KCNQ‐SMIT complex formation facilitates ion channel‐solute transporter cross talk

2017 ◽  
Vol 31 (7) ◽  
pp. 2828-2838 ◽  
Author(s):  
Daniel L. Neverisky ◽  
Geoffrey W. Abbott
Keyword(s):  
Complex Formation ◽  
Ion Channel ◽  
Cross Talk ◽  
Solute Transporter

scholarly journals Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation

2012 ◽  
Vol 41 (1) ◽  
pp. 327-339 ◽  
Author(s):  
Paola Cavaliere ◽  
Bruno Pagano ◽  
Vincenzo Granata ◽  
Stephanie Prigent ◽  
Human Rezaei ◽  
...  
Keyword(s):  
Complex Formation ◽  
Nucleic Acids ◽  
Prion Protein ◽  
Cross Talk

scholarly journals Ion Channel-Forming Alamethicin Is a Potent Elicitor of Volatile Biosynthesis and Tendril Coiling. Cross Talk between Jasmonate and Salicylate Signaling in Lima Bean

2001 ◽  
Vol 125 (1) ◽  
pp. 369-377 ◽  
Author(s):  
Jürgen Engelberth ◽  
Thomas Koch ◽  
Göde Schüler ◽  
Nadine Bachmann ◽  
Jana Rechtenbach ◽  
...  
Keyword(s):  
Ion Channel ◽  
Cross Talk ◽  
Lima Bean ◽  
Tendril Coiling

Peripheral 5-HT3 mediates mirror-image pain by a cross-talk with acid-sensing ion channel 3

2018 ◽  
Vol 130 ◽  
pp. 92-104 ◽  
Author(s):  
Yeu-Shiuan Su ◽  
Hao-Ruei Mei ◽  
Chun-Hung Wang ◽  
Wei-Hsin Sun
Keyword(s):  
Ion Channel ◽  
Cross Talk ◽  
Mirror Image

scholarly journals Cross-talk between Integrin α6β4 and Insulin-like Growth Factor-1 Receptor (IGF1R) through Direct α6β4 Binding to IGF1 and Subsequent α6β4-IGF1-IGF1R Ternary Complex Formation in Anchorage-independent Conditions

2012 ◽  
Vol 287 (15) ◽  
pp. 12491-12500 ◽  
Author(s):  
Masaaki Fujita ◽  
Katsuaki Ieguchi ◽  
Parastoo Davari ◽  
Satoshi Yamaji ◽  
Yukimasa Taniguchi ◽  
...  
Keyword(s):  
Growth Factor ◽  
Complex Formation ◽  
Cross Talk ◽  
Intracellular Signaling ◽  
Ternary Complex ◽  
Dependent Manner ◽  
Insulin Like Growth Factor ◽  
Ternary Complex Formation ◽  
Integrin Α6β4 ◽  
Igf Signaling

Integrin αvβ3 plays a role in insulin-like growth factor-1 (IGF1) signaling (integrin-IGF1 receptor (IGF1R) cross-talk). The specifics of the cross-talk are, however, unclear. In a current model, “ligand occupancy” of αvβ3 (i.e. the binding of extracellular matrix proteins) enhances signaling induced by IGF1 binding to IGF1R. We recently reported that IGF1 directly binds to αvβ3 and induces αvβ3-IGF1-IGF1R ternary complex formation. Consistently, the integrin binding-defective IGF1 mutant (R36E/R37E) is defective in inducing ternary complex formation and IGF signaling, but it still binds to IGF1R. Like αvβ3, integrin α6β4 is overexpressed in many cancers and is implicated in cancer progression. Here, we discovered that α6β4 directly bound to IGF1, but not to R36E/R37E. Grafting the β4 sequence WPNSDP (residues 167–172), which corresponds to the specificity loop of β3, to integrin β1 markedly enhanced IGF1 binding to β1, suggesting that the WPNSDP sequence is involved in IGF1 recognition. WT IGF1 induced α6β4-IGF1-IGF1R ternary complex formation, whereas R36E/R37E did not. When cells were attached to matrix, exogenous IGF1 or α6β4 expression had little or no effect on intracellular signaling. When cell-matrix adhesion was reduced (in poly(2-hydroxyethyl methacrylate-coated plates), IGF1 induced intracellular signaling and enhanced cell survival in an α6β4-dependent manner. Also IGF1 enhanced colony formation in soft agar in an α6β4-dependent manner. These results suggest that IGF binding to α6β4 plays a major role in IGF signaling in anchorage-independent conditions, which mimic the in vivo environment, and is a novel therapeutic target.

scholarly journals Signaling from mTOR to eIF2α mediates cell migration in response to the chemotherapeutic doxorubicin

2019 ◽  
Vol 12 (612) ◽  
pp. eaaw6763 ◽  
Author(s):  
Robert F. Harvey ◽  
Tuija A. A. Pöyry ◽  
Mark Stoneley ◽  
Anne E. Willis
Keyword(s):  
Cell Migration ◽  
Complex Formation ◽  
Cross Talk ◽  
Ternary Complex ◽  
Complex Compounds ◽  
Initiation Factor ◽  
Patients With Cancer ◽  
Eif2α Phosphorylation ◽  
Cell Metastasis ◽  
Promote Cell Survival

After exposure to cytotoxic chemotherapeutics, tumor cells alter their translatome to promote cell survival programs through the regulation of eukaryotic initiation factor 4F (eIF4F) and ternary complex. Compounds that block mTOR signaling and eIF4F complex formation, such as rapamycin and its analogs, have been used in combination therapies to enhance cell killing, although their success has been limited. This is likely because the cross-talk between signaling pathways that coordinate eIF4F regulation with ternary complex formation after treatment with genotoxic therapeutics has not been fully explored. Here, we described a regulatory pathway downstream of p53 in which inhibition of mTOR after DNA damage promoted cross-talk signaling and led to eIF2α phosphorylation. We showed that eIF2α phosphorylation did not inhibit protein synthesis but was instead required for cell migration and that pharmacologically blocking this pathway with either ISRIB or trazodone limited cell migration. These results support the notion that therapeutic targeting of eIF2α signaling could restrict tumor cell metastasis and invasion and could be beneficial to subsets of patients with cancer.

„Cross-talk“ zwischen Herz und Niere – das Kardiorenale Syndrom und seine Therapie aus der Sicht des Nephrologen

2009 ◽  
Vol 66 (11) ◽  
pp. 741-746 ◽  
Author(s):  
Stefan Farese
Keyword(s):  
Cross Talk

Herz und Nierenfunktion sind eng miteinander verknüpft. Ein Großteil der Patienten mit chronischer Herzinsuffizienz leidet gleichzeitig an einer Nierenfunktionsstörung. Diese ist kausal an der Entwicklung der Herzinsuffizienz beteiligt und stellt damit einen wichtigen prognostischen Faktor dar. Pathophysiologisch kommt es durch die verminderte renale Perfusion zu einer Aktivierung verschiedener Regelkreise, die eine Salz- und Wasserretention induzieren und damit das Fortschreiten der Herzinsuffizienz begünstigen. Therapeutische Ziele sind die Euvolämie sowie die kontrollierte Behandlung mittels prognostisch relevanter, kardialer Begleitmedikation. Können diese beiden Ziele aufgrund von Therapieresistenz, progredienter Niereninsuffizienz oder Therapie-Nebenwirkungen nicht erreicht werden, ist die Indikation für ein Nierenersatzverfahren gegeben. Prinzipiell können alle heute verfügbaren Verfahren angewendet werden. Die Auswahl der Modalität sollte jedoch an die individuelle Situation des Patienten angepasst und interdisziplinär besprochen werden. Obwohl sich unter Therapie bei allen Nierenersatzverfahren funktionelle und subjektive Verbesserungen nachweisen lassen, ist deren Einfluss auf die Langzeitprognose ungeklärt.

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