Dissection of the promoter region of the inositol 1,4,5-trisphosphate receptor gene, itr-1, in C. elegans: a molecular basis for cell-specific expression of IP3R isoforms11Edited by J. Karn

2001 ◽  
Vol 306 (2) ◽  
pp. 145-157 ◽  
Author(s):  
Nicholas J.D Gower ◽  
Gillian R Temple ◽  
Jacqueline E Schein ◽  
Marco Marra ◽  
Denise S Walker ◽  
...  
Gene ◽  
1997 ◽  
Vol 196 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Kiyoshi Morikawa ◽  
Tetsuya Ohbayashi ◽  
Midori Nakagawa ◽  
Yoshiyuki Konishi ◽  
Yasutaka Makino ◽  
...  

1997 ◽  
Vol 17 (2) ◽  
pp. 635-645 ◽  
Author(s):  
Valerie A. Street ◽  
Martha M. Bosma ◽  
Vasiliki P. Demas ◽  
Melissa R. Regan ◽  
Doras D. Lin ◽  
...  

Genome ◽  
1996 ◽  
Vol 39 (2) ◽  
pp. 456-458 ◽  
Author(s):  
Silja Kostia ◽  
Jukka Palo ◽  
Sirkka-Liisa Varvio

A bovine RAPD profile, generated by a 10-mer primer, was analysed by sequencing the major fragments. Three of four different fragments showed homologies to previously characterized mammalian sequences. One was 61–66% identical to LINE sequences and another was 78.5% identical to a human chromosome 2 sequence tagged site. The third fragment was 93.1% identical to the human type 2 inositol 1,4,5-trisphosphate receptor gene. This fragment had counterparts in white-tailed deer and reindeer; fragments of slightly different size in these species showed high sequence similarity and the size differences were due to varying numbers of dinucleotide microsatellite repeats inside the fragment. Key words : RAPD, artiodactyls, sequence similarity, microsatellites, type 2 inositol 1,4,5-trisphosphate receptor.


2002 ◽  
Vol 13 (4) ◽  
pp. 1329-1337 ◽  
Author(s):  
Denise S. Walker ◽  
Nicholas J.D. Gower ◽  
Sung Ly ◽  
Gemma L. Bradley ◽  
Howard A. Baylis

Inositol 1,4,5-trisphosphate (IP3) is an important second messenger in animal cells and is central to a wide range of cellular responses. The major intracellular activity of IP3 is to regulate release of Ca2+ from intracellular stores through IP3 receptors (IP3Rs). We describe a system for the transient disruption of IP3 signaling in the model organismCaenorhabditis elegans. The IP3 binding domain of the C. elegans IP3R, ITR-1, was expressed from heat shock-induced promoters in live animals. This results in a dominant-negative effect caused by the overexpressed IP3 binding domain acting as an IP3“sponge.” Disruption of IP3 signaling resulted in disrupted defecation, a phenotype predicted by previous genetic studies. This approach also identified two new IP3-mediated processes. First, the up-regulation of pharyngeal pumping in response to food is dependent on IP3 signaling. RNA-mediated interference studies and analysis of itr-1mutants show that this process is also IP3R dependent. Second, the tissue-specific expression of the dominant-negative construct enabled us to circumvent the sterility associated with loss of IP3 signaling through the IP3R and thus determine that IP3-mediated signaling is required for multiple steps in embryogenesis, including cytokinesis and gastrulation.


2004 ◽  
Vol 15 (8) ◽  
pp. 3938-3949 ◽  
Author(s):  
Xiaoyan Yin ◽  
Nicholas J.D. Gower ◽  
Howard A. Baylis ◽  
Kevin Strange

Intercellular communication between germ cells and neighboring somatic cells is essential for reproduction. Caenorhabditis elegans oocytes are surrounded by and coupled via gap junctions to smooth muscle-like myoepithelial sheath cells. Rhythmic sheath cell contraction drives ovulation and is triggered by a factor secreted from oocytes undergoing meiotic maturation. We demonstrate for the first time that signaling through the epidermal growth factor-like ligand LIN-3 and the LET-23 tyrosine kinase receptor induces ovulatory contractions of sheath cells. Reduction-of-function mutations in the inositol 1,4,5-trisphosphate (IP3) receptor gene itr-1 and knockdown of itr-1 expression by RNA interference inhibit sheath contractile activity. itr-1 gain-of-function mutations increase the rate and force of basal contractions and induce tonic sheath contraction during ovulation. Sheath contractile activity is disrupted by RNAi of plc-3, one of six phospholipase C-encoding genes in the C. elegans genome. PLC-3 is a PLC-γ homolog and is expressed in contractile sheath cells of the proximal gonad. Maintenance of sheath contractile activity requires plasma membrane Ca2+ entry. We conclude that IP3 generated by LET-23 mediated activation of PLC-γ induces repetitive intracellular Ca2+ release that drives rhythmic sheath cell contraction. Calcium entry may function to trigger Ca2+ release via IP3 receptors and/or refill intracellular Ca2+ stores.


2003 ◽  
Vol 350 (2) ◽  
pp. 69-72 ◽  
Author(s):  
Takeshi Aoki ◽  
Minoru Narita ◽  
Orie Ohnishi ◽  
Keisuke Mizuo ◽  
Michiko Narita ◽  
...  

2001 ◽  
Vol 72 (4) ◽  
pp. 1717-1724 ◽  
Author(s):  
Yoshiyuki Konishi ◽  
Noriaki Ohkawa ◽  
Yasutaka Makino ◽  
Hiroaki Ohkubo ◽  
Ryoichiro Kageyama ◽  
...  

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