scholarly journals lin-8, Which Antagonizes Caenorhabditis elegans Ras-Mediated Vulval Induction, Encodes a Novel Nuclear Protein That Interacts With the LIN-35 Rb Protein

Genetics ◽  
2005 ◽  
Vol 171 (3) ◽  
pp. 1017-1031 ◽  
Author(s):  
Ewa M. Davison ◽  
Melissa M. Harrison ◽  
Albertha J. M. Walhout ◽  
Marc Vidal ◽  
H. Robert Horvitz
Keyword(s):  
Caenorhabditis Elegans ◽  
Nuclear Protein ◽  
Rb Protein

Characterization of STIP, a multi-domain nuclear protein, highly conserved in metazoans, and essential for embryogenesis in Caenorhabditis elegans

2007 ◽  
Vol 313 (7) ◽  
pp. 1460-1472 ◽  
Author(s):  
Qiongmei Ji ◽  
Cheng-Han Huang ◽  
Jianbin Peng ◽  
Sarwar Hashmi ◽  
Tianzhang Ye ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Nuclear Protein

scholarly journals The Caenorhabditis elegans Gene mfap-1 Encodes a Nuclear Protein That Affects Alternative Splicing

PLoS Genetics ◽  
2012 ◽  
Vol 8 (7) ◽  
pp. e1002827 ◽  
Author(s):  
Long Ma ◽  
Xiaoyang Gao ◽  
Jintao Luo ◽  
Liange Huang ◽  
Yanling Teng ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Caenorhabditis Elegans ◽  
Nuclear Protein

scholarly journals SMU-2 and SMU-1, Caenorhabditis elegans Homologs of Mammalian Spliceosome-Associated Proteins RED and fSAP57, Work Together To Affect Splice Site Choice

2004 ◽  
Vol 24 (15) ◽  
pp. 6811-6823 ◽  
Author(s):  
Angela K. Spartz ◽  
Robert K. Herman ◽  
Jocelyn E. Shaw
Keyword(s):  
Caenorhabditis Elegans ◽  
Splice Site ◽  
Nuclear Protein ◽  
Core Protein ◽  
Protein A ◽  
Nonsense Mutations ◽  
Associated Proteins ◽  
Mutant Phenotypes

ABSTRACT Mutations in the Caenorhabditis elegans gene smu-2 suppress mec-8 and unc-52 mutations. It has been proposed that MEC-8 regulates the alternative splicing of unc-52 transcripts, which encode the core protein of perlecan, a basement membrane proteoglycan. We show that mutation in smu-2 leads to enhanced accumulation of transcripts that skip exon 17, but not exon 18, of unc-52, which explains our finding that smu-2 mutations suppress the uncoordination conferred by nonsense mutations in exon 17, but not in exon 18, of unc-52. We conclude that smu-2 encodes a ubiquitously expressed nuclear protein that is 40% identical to the human RED protein, a component of purified spliceosomes. The effects of smu-2 mutation on both unc-52 pre-mRNA splicing and the suppression of mec-8 and unc-52 mutant phenotypes are indistinguishable from the effects of mutation in smu-1, a gene that encodes a protein that is 62% identical to human spliceosome-associated protein fSAP57. We provide evidence that SMU-2 protects SMU-1 from degradation in vivo. In vitro and in vivo coimmunoprecipitation experiments indicate that SMU-2 and SMU-1 bind to each other. We propose that SMU-2 and SMU-1 function together to regulate splice site choice in the pre-mRNAs of unc-52 and other genes.

CHR3: a Caenorhabditis elegans orphan nuclear hormone receptor required for proper epidermal development and molting

Development ◽  
1998 ◽  
Vol 125 (9) ◽  
pp. 1617-1626 ◽  
Author(s):  
M. Kostrouchova ◽  
M. Krause ◽  
Z. Kostrouch ◽  
J.E. Rall
Keyword(s):  
Caenorhabditis Elegans ◽  
Hormone Receptor ◽  
Nuclear Protein ◽  
Cell Function ◽  
Reporter Genes ◽  
Postembryonic Development ◽  
Nuclear Hormone Receptor ◽  
Hormone Response ◽  
Gene Encoding ◽  
Inducible Gene

CHR3 is a Caenorhabditis elegans orphan nuclear hormone receptor highly homologous to Drosophila DHR3, an ecdysone-inducible gene product involved in metamorphosis. Related vertebrate factors include RORalpha/RZRalpha, RZRbeta and RevErb. Gel-shift studies show that CHR3 can bind the DR5-type hormone response sequence. CHR3 is a nuclear protein present in all blastomeres during early embryogenesis. During morphogenesis, both CHR3 protein and zygotically active reporter genes are detectable in epidermal cells and their precursors. Inhibition of the gene encoding CHR3 results in several larval defects associated with abnormal epidermal cell function, including molting and body size regulation, suggesting that CHR3 is an essential epidermal factor required for proper postembryonic development.

The C. elegans gene lin-36 acts cell autonomously in the lin-35 Rb pathway

Development ◽  
1999 ◽  
Vol 126 (15) ◽  
pp. 3449-3459 ◽  
Author(s):  
J.H. Thomas ◽  
H.R. Horvitz
Keyword(s):  
Amino Acids ◽  
Caenorhabditis Elegans ◽  
Tyrosine Kinase ◽  
Receptor Tyrosine Kinase ◽  
Intercellular Signaling ◽  
Rb Protein ◽  
C Elegans ◽  
Rb Pathway ◽  
Vulval Precursor Cells ◽  
Novel Protein

The Caenorhabditis elegans gene lin-36 acts to antagonize Ras-mediated vulval induction in a pathway that includes genes with products similar to the mammalian retinoblastoma (Rb) protein and the Rb-binding protein p48. We report that lin-36 encodes a novel protein of 962 amino acids. We demonstrate that lin-36 functions in and is expressed in the vulval precursor cells, establishing that the lin-36 pathway is involved in intercellular signaling. We also report that the lin-36 pathway and/or another pathway that is functionally redundant with the lin-36 pathway antagonize a ligand-independent activity of the receptor tyrosine kinase/Ras vulval induction pathway.

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