Walter PL [class:all]
[species:All Species]
[species:All Species]
- Download all ()
- Classes
- Classes
- Anatomy term:
- Antibody:
- CDS:
- Clone:
- Construct:
- Expression pattern:
- Expression profile:
- Expression cluster:
- Sequence feature:
- Gene:
- Gene cluster:
- Genotype:
- GO term:
- Homology group:
- Interaction:
- Life stage:
- Microarray results:
- Operon:
- PCR Product/Oligo:
- Phenotype:
- Position matrix:
- Protein:
- Pseudogene:
- Rearrangement:
- RNAi:
- Sequence:
- Strain:
- Structure Data:
- Transcript:
- Transgene:
- Transposon:
- Variation:
- Analysis:
- Disease Ontology:
- Gene class:
- Laboratory:
- Molecule:
- Motif:
- Paper:
- Person:
- Picture:
- Reagent:
- Transposon Family:
- Process&Pathway:
- Paper types
- Paper types
- Journal article:
- Review:
- Lectures:
- Interactive tutorial:
- Retracted publication:
- Technical report:
- Directory:
- Monograph:
- Published erratum:
- Meeting abstract:
- Gazette article:
- Book chapter:
- Comment:
- Book:
- Email:
- WormBook:
- Other:
- News:
- Letter:
- Editorial:
- Congresses:
- Historical article:
- Biography:
- Interview:
- Species
91 results (0.01 seconds)
- paper:
- antibody: WBAntibody00002815
- paper:
- paper:
- paper:
[
Arch Biochem Biophys,
2006] Cells respond to heavy metal stress by activating signaling cascades regulating cellular proliferation and survival. We here demonstrate that the anti-apoptotic kinase Akt is activated in HepG2 human hepatoma cells exposed to copper or zinc ions. Cu(2+)- and Zn(2+)-induced phosphorylation of Akt was blocked by phosphoinositide 3-kinase (PI3K) inhibitors, wortmannin and LY294002. Moreover, several endogenous Akt substrates were phosphorylated, including glycogen synthase kinase-3 and transcription factors of the FoxO family, FoxO1a and FoxO4. Exposure to Cu(2+) or Zn(2+) elicited the subcellular redistribution of an overexpressed FoxO1a-EGFP fusion protein from nucleus to cytoplasm, which was not seen with a mutant FoxO1a form devoid of Akt phosphorylation sites. Both FoxO phosphorylation and nuclear exclusion were blocked by wortmannin. Likewise, the subcellular translocation from nucleus to cytoplasm of the Caenorhabditis elegans FoxO ortholog, DAF-16, was caused in starved worms exposed to copper ions. Activity of the promoter of the human glucose 6-phosphatase gene, known to be regulated by insulin and FoxO1a, was demonstrated in reporter gene assays to be attenuated in hepatoma cells exposed to Cu(2+). However, this suppression of glucose 6-phosphatase promoter activity was independent of modulation of the PI3K/Akt pathway. In summary, the PI3K/Akt pathway is activated in human hepatoma cells exposed to Cu(2+) or Zn(2+), resulting in the phosphorylation and subcellular relocalisation of transcription factor FoxO1a. Furthermore, copper is demonstrated to exert an insulin-mimetic effect also independently of the PI3K/Akt/FoxO pathway.
Rabbit-SYP-1_3Phos antibodies generated using the phosphopeptide [SAPLM(pT) S(pT)PL(pT)AATR] syp-1
[
J Biol Chem,
1997] The rapid movement of phospholipids (PL) between plasma membrane leaflets in response to increased intracellular Ca2+ is thought to play a key role in expression of platelet procoagulant activity and in clearance of injured or apoptotic cells. We recently reported isolation of a approximately 37-kDa protein in erythrocyte membrane that mediates Ca2+-dependent movement of PL between membrane leaflets, similar to that observed upon elevation of Ca2+ in the cytosol (Basse, F., Stout, J. G., Sims, P. J., and Wiedmer, T. (1996) J. Biol. Chem. 271, 17205-17210). Based on internal peptide sequence obtained from this protein, a 1,445-base pair cDNA was cloned from a K-562 cDNA library. The deduced "PL scramblase" protein is a proline-rich, type II plasma membrane protein with a single transmembrane segment near the C terminus. Antibody against the deduced C-terminal peptide was found to precipitate the approximately 37-kDa red blood cell protein and absorb PL scramblase activity, confirming the identity of the cloned cDNA to erythrocyte PL scramblase. Ca2+-dependent PL scramblase activity was also demonstrated in recombinant protein expressed from plasmid containing the cDNA. Quantitative immunoblotting revealed an approximately 10-fold higher abundance of PL scramblase in platelet ( approximately 10(4) molecules/cell) than in erythrocyte ( approximately 10(3) molecules/cell), consistent with apparent increased PL scramblase activity of the platelet plasma membrane. PL scramblase mRNA was found in a variety of hematologic and nonhematologic cells and tissues, suggesting that this protein functions in all cells.
[
STAR Protoc,
2021] Enzyme-catalyzed proximity labeling (PL) has emerged as a critical approach for identifying protein-protein proximity interactions in cells; however, PL techniques were not historically practical in living multicellular organisms due to technical limitations. Here, we present a protocol for applying PL to living <i>C.elegans</i> using the biotin ligase mutant enzyme TurboID. We demonstrated PL in a tissue-specific and region-specific manner by focusing on non-centrosomal MTOCs (ncMTOCs) of intestinal cells. This protocol is useful for targeted <i>in vivo</i> protein network profiling. For complete details on the use and execution of this protocol, please refer to Sanchez et al. (2021).
[
East Coast Worm Meeting,
2000] We are analyzing a sexually dimorphic appetitive behavior in C. elegans. Hermaphrodites placed on a food source will forage and lay eggs, rarely wandering away from the food. In contrast, individual males cultured in the absence of hermaphrodites will wander away from food - a behavior we refer to as "leaving." We have developed a quantitative leaving assay with the intention of dissecting the molecular mechanisms governing both sex drive and the interactions between the sexes. Animals are placed singly on a small bacterial lawn in the center of a 9cm plate. A worm that has wandered as far as 3.5 cm from the plate's center, or off the plate entirely, is scored as a leaver. We have found that leaving can be modeled as a stochastic process characterized by probability of leaving per hour (PL). For wild-type males, PL is 0.1 whereas for hermaphrodites, PL is 0. PL(male) is independent of time separated from hermaphrodites, indicating that males do not become motivated to leave with mating deprivation. PL is also independent of prior mating experience. Plating males with hermaphrodites completely abrogates leaving whereas plating males with males, does not. Males plated with hermaphrodites for several hours leave instantaneously upon hermaphrodite removal and with PL commensurate to males plated alone. This result suggests both that sexual experience does not affect leaving behavior and that a putative hermaphrodite-derived signal is short-lived. lin-39, let-23, and lin-4 hermaphrodites were also capable of attenuating leaving suggesting that neither the vulva nor successful copulation are required to "keep" males. PL for mab-3(e1240) males plated with hermaphrodites resembled that of males plated alone, suggesting that mab-3 is required for males to respond to hermaphrodites. We have found that neither L4 males nor L4 hermaphrodites leave (PL is 0); male leaving commences with the onset of sexual maturity. Neither dopamine- nor serotonin-deficient mutants showed significant alterations in leaving behavior. We screened for mutants with decreased PL(male). Several lad (leaving assay defective) mutants have been isolated. PL of lad-1 males is approximately 0. Although lad-1 males do not appreciably leave food, they move well, mate, and are morphologically wild-type.
load 10 more results
