scholarly journals Spatio-temporal regulation and cleavage by matrix metalloproteinase stromelysin-3 implicate a role for laminin receptor in intestinal remodeling duringXenopus laevis metamorphosis

2005 ◽  
Vol 234 (1) ◽  
pp. 190-200 ◽  
Author(s):  
Tosikazu Amano ◽  
Liezhen Fu ◽  
Anastasia Marshak ◽  
Olivia Kwak ◽  
Yun-Bo Shi
Keyword(s):  
Matrix Metalloproteinase ◽  
Laminin Receptor ◽  
Temporal Regulation ◽  
Spatio Temporal ◽  
Intestinal Remodeling ◽  
Stromelysin 3

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

Deciphering the spatio-temporal regulation of entry and progression through mitosis

2014 ◽  
Vol 9 (2) ◽  
pp. 213-223 ◽  
Author(s):  
Lilia Gheghiani ◽  
Olivier Gavet
Keyword(s):  
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.

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