scholarly journals Spatio-temporal regulation of EGFR signaling by the Eps15 homology domain-containing protein 3 (EHD3)

Oncotarget ◽  
2016 ◽  
Vol 7 (48) ◽  
pp. 79203-79216 ◽  
Author(s):  
Mohamed Amessou ◽  
Abdul Shukkur Ebrahim ◽  
Ashok Dilly ◽  
Melvin Joseph ◽  
Marina Tabolina ◽  
...  
Keyword(s):  
Egfr Signaling ◽  
Temporal Regulation ◽  
Spatio Temporal ◽  
Eps15 Homology Domain

scholarly journals P-bodies and the miRNA pathway regulate translational repression of bicoid mRNA during Drosophila melanogaster oogenesis

2018 ◽  
Author(s):  
John M. McLaughlin ◽  
Daniel F.Q. Smith ◽  
Irina E. Catrina ◽  
Diana P. Bratu
Keyword(s):  
Drosophila Melanogaster ◽  
Small Rna ◽  
Translational Regulation ◽  
Translational Repression ◽  
Temporal Regulation ◽  
P Bodies ◽  
Maternal Transcripts ◽  
Spatio Temporal ◽  
Mirna Pathway ◽  
Rna Pathways

ABSTRACTEmbryonic axis patterning in Drosophila melanogaster is partly achieved by mRNAs that are maternally localized to the oocyte; the spatio-temporal regulation of these transcripts’ stability and translation is a characteristic feature of oogenesis. While protein regulatory factors are necessary for the translational regulation of some maternal transcripts (e.g. oskar and gurken), small RNA pathways are also known to regulate mRNA stability and translation in eukaryotes. MicroRNAs (miRNAs) are small RNA regulators of gene expression, widely conserved throughout eukaryotic genomes and essential for animal development. The main D. melanogaster anterior determinant, bicoid, is maternally transcribed, but it is not translated until early embryogenesis. We investigated the possibility that its translational repression during oogenesis is mediated by miRNA activity. We found that the bicoid 3’UTR contains a highly conserved, predicted binding site for miR-305. Our studies reveal that miR-305 regulates the translation of a reporter gene containing the bicoid 3’UTR in cell culture, and that miR-305 only partially contributes to bicoid mRNA translational repression during oogenesis. We also found that Processing bodies (P-bodies) in the egg chamber may play a role in stabilizing bicoid and other maternal transcripts. Here, we offer insights into the possible role of P-bodies and the miRNA pathway in the translational repression of bicoid mRNA during oogenesis.

scholarly journals Spatio-temporal regulation of calpain activity after experimental myocardial infarction in vivo

2021 ◽  
Vol 28 ◽  
pp. 101162
Author(s):  
Kun Zhang ◽  
Melissa M. Cremers ◽  
Stephan Wiedemann ◽  
David M. Poitz ◽  
Christian Pfluecke ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Experimental Myocardial Infarction ◽  
Calpain Activity ◽  
Temporal Regulation ◽  
Spatio Temporal

scholarly journals Apical polarity proteins recruit the RhoGEF Cysts to promote junctional myosin assembly

2019 ◽  
Vol 218 (10) ◽  
pp. 3397-3414 ◽  
Author(s):  
Jordan T. Silver ◽  
Frederik Wirtz-Peitz ◽  
Sérgio Simões ◽  
Milena Pellikka ◽  
Dong Yan ◽  
...  
Keyword(s):  
Rho Gtpases ◽  
Rho Gtpase ◽  
Adherens Junctions ◽  
Nucleotide Exchange ◽  
Temporal Regulation ◽  
Apical Polarity ◽  
Polarity Proteins ◽  
Spatio Temporal ◽  
Crumbs Complex

The spatio-temporal regulation of small Rho GTPases is crucial for the dynamic stability of epithelial tissues. However, how RhoGTPase activity is controlled during development remains largely unknown. To explore the regulation of Rho GTPases in vivo, we analyzed the Rho GTPase guanine nucleotide exchange factor (RhoGEF) Cysts, the Drosophila orthologue of mammalian p114RhoGEF, GEF-H1, p190RhoGEF, and AKAP-13. Loss of Cysts causes a phenotype that closely resembles the mutant phenotype of the apical polarity regulator Crumbs. This phenotype can be suppressed by the loss of basolateral polarity proteins, suggesting that Cysts is an integral component of the apical polarity protein network. We demonstrate that Cysts is recruited to the apico-lateral membrane through interactions with the Crumbs complex and Bazooka/Par3. Cysts activates Rho1 at adherens junctions and stabilizes junctional myosin. Junctional myosin depletion is similar in Cysts- and Crumbs-compromised embryos. Together, our findings indicate that Cysts is a downstream effector of the Crumbs complex and links apical polarity proteins to Rho1 and myosin activation at adherens junctions, supporting junctional integrity and epithelial polarity.

scholarly journals The scaffold-protein IQGAP1 enhances and spatially restricts the actin-nucleating activity of Diaphanous-related formin 1 (DIAPH1)

2020 ◽  
Vol 295 (10) ◽  
pp. 3134-3147 ◽  
Author(s):  
Anan Chen ◽  
Pam D. Arora ◽  
Christine C. Lai ◽  
John W. Copeland ◽  
Trevor F. Moraes ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Actin Filament ◽  
Intramolecular Interaction ◽  
Essential Feature ◽  
Temporal Regulation ◽  
Iq Motif ◽  
Sequential Binding ◽  
Spatio Temporal

The actin cytoskeleton is a dynamic array of filaments that undergoes rapid remodeling to drive many cellular processes. An essential feature of filament remodeling is the spatio-temporal regulation of actin filament nucleation. One family of actin filament nucleators, the Diaphanous-related formins, is activated by the binding of small G-proteins such as RhoA. However, RhoA only partially activates formins, suggesting that additional factors are required to fully activate the formin. Here we identify one such factor, IQ motif containing GTPase activating protein-1 (IQGAP1), which enhances RhoA-mediated activation of the Diaphanous-related formin (DIAPH1) and targets DIAPH1 to the plasma membrane. We find that the inhibitory intramolecular interaction within DIAPH1 is disrupted by the sequential binding of RhoA and IQGAP1. Binding of RhoA and IQGAP1 robustly stimulates DIAPH1-mediated actin filament nucleation in vitro. In contrast, the actin capping protein Flightless-I, in conjunction with RhoA, only weakly stimulates DIAPH1 activity. IQGAP1, but not Flightless-I, is required to recruit DIAPH1 to the plasma membrane where actin filaments are generated. These results indicate that IQGAP1 enhances RhoA-mediated activation of DIAPH1 in vivo. Collectively these data support a model where the combined action of RhoA and an enhancer ensures the spatio-temporal regulation of actin nucleation to stimulate robust and localized actin filament production in vivo.

scholarly journals Differential spatio-temporal regulation of MMPs in the 5xFAD mouse model of Alzheimer’s disease: evidence for a pro-amyloidogenic role of MT1-MMP

2014 ◽  
Vol 6 ◽  
Author(s):  
Nathalie A. Py ◽  
Amandine E. Bonnet ◽  
Anne Bernard ◽  
Yannick Marchalant ◽  
Eliane Charrat ◽  
...  
Keyword(s):  
Mouse Model ◽  
Temporal Regulation ◽  
5Xfad Mouse ◽  
Spatio Temporal
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