New Findings in Ubiquitins Described from National Center for Scientific Research (CNRS) (RPM-1 Uses Both Ubiquitin Ligase and Phosphatase-Based...

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New Findings in Ubiquitins Described from National Center for Scientific Research (CNRS) (RPM-1 Uses Both Ubiquitin Ligase and Phosphatase-Based Mechanisms to Regulate DLK-1 during Neuronal Development) By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteins are discussed in a new report. According to news originating from Gif sur Yvette, France, by NewsRx correspondents, research stated, "The Pam/Highwire/RPM-1 (PHR) proteins are key regulators of neuronal development that function in axon extension and guidance, termination of axon outgrowth, and synapse formation. Outside of development, the PHR proteins also regulate axon regeneration and Wallerian degeneration." Our news journalists obtained a quote from the research from National Center for Scientific Research (CNRS), "The PHR proteins function in part by acting as ubiquitin ligases that degrade the Dual Leucine zipper-bearing Kinase (DLK). Here, we show that the Caenorhabditis elegans PHR protein, Regulator of Presynaptic Morphology 1 (RPM-1), also utilizes a phosphatase-based mechanism to regulate DLK-1. Using mass spectrometry, we identified Protein Phosphatase Magnesium/Manganese dependent 2 (PPM-2) as a novel RPM-1 binding protein. Genetic, transgenic, and biochemical studies indicated that PPM-2 functions coordinately with the ubiquitin ligase activity of RPM-1 and the F-box protein FSN-1 to negatively regulate DLK-1. PPM-2 acts on S874 of DLK-1, a residue implicated in regulation of DLK-1 binding to a short, inhibitory isoform of DLK-1 (DLK-1S). Our study demonstrates that PHR proteins function through both phosphatase and ubiquitin ligase mechanisms to inhibit DLK. Thus, PHR proteins are potentially more accurate and sensitive regulators of DLK than originally thought." According to the news editors, the research concluded: "Our results also highlight an important and expanding role for the PP2C phosphatase family in neuronal development." For more information on this research see: RPM-1 Uses Both Ubiquitin Ligase and Phosphatase-Based Mechanisms to Regulate DLK-1 during Neuronal Development. PLoS Genetics, 2014;10(5):84-101. PLoS Genetics can be contacted at: Public Library Science, 1160 Battery Street, Ste 100, San Francisco, CA 94111, USA. (Public Library of Science - www.plos.org; PLoS Genetics - www.plosgenetics.org) The news correspondents report that additional information may be obtained from S.T. Baker, CNRS, Gif Sur Yvette, France. Additional authors for this research include K.J. Opperman, E.D. Tulgren, S.M. Turgeon, W. Bienvenut and B. Grill (see also Proteins). Keywords for this news article include: France, Europe, Ligases, Proteins, Ubiquitins, Gif sur Yvette, Enzymes and Coenzymes Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC

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