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Molecular & Cellular Proteomics

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Plant Biology*

  • The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome
    Open Access
    The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome
    Fatima Haj Ahmad, Xu Na Wu, Annick Stintzi, Andreas Schaller and Waltraud X. Schulze
    Molecular & Cellular Proteomics August 1, 2019, First published on May 28, 2019, 18 (8) 1526-1542; https://doi.org/10.1074/mcp.RA119.001367

    The early phosphorylation signaling cascade of the peptide hormone systemin was defined through comparing systemin-induced responses with non-specific responses induced by the inactive analogon systemin-A17 or mock treatment. Systemin-responsive phosphorylation of kinases and phosphatases was identified over a time course of 2 to 45 minutes, as well as typical substrate phosphorylation sites. We identified the C-terminal threonine of H+-ATPase LHA1 as a substrate of phosphatase PLL5 and MAP-Kinase MPK2, thereby defining a signaling circuit of rapid dephosphorylation and re-phosphorylation after 15 minutes.

  • Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain
    Open Access
    Sucrose-induced Receptor Kinase 1 is Modulated by an Interacting Kinase with Short Extracellular Domain
    Xu Na Wu, Liangcui Chu, Lin Xi, Heidi Pertl-Obermeyer, Zhi Li, Kamil Sklodowski, Clara Sanchez-Rodriguez, Gerhard Obermeyer and Waltraud X. Schulze
    Molecular & Cellular Proteomics August 1, 2019, First published on May 30, 2019, 18 (8) 1556-1571; https://doi.org/10.1074/mcp.RA119.001336

    The activation of aquaporins by a receptor kinase complex of SIRK1 and QSK1 was studied in detail. Based on phosphoproteomics, pulldown studies and physiological experiments we conclude that SIRK1 may function as a main receptor which forms a complex with coreceptor QSK1. SIRK1 can autophosphorylate and then trans-phosphorylate QSK1. Phosphorylated QSK1 enhanced and stabilized the interaction with aquaporins as substrates of the receptor kinase complex.

  • A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition
    Open Access
    A Label-free Mass Spectrometry Method to Predict Endogenous Protein Complex Composition
    Zachary McBride, Donglai Chen, Youngwoo Lee, Uma K. Aryal, Jun Xie and Daniel B. Szymanski
    Molecular & Cellular Proteomics August 1, 2019, First published on June 11, 2019, 18 (8) 1588-1606; https://doi.org/10.1074/mcp.RA119.001400

    At least one third of soluble proteins are predicted to exist in a stable oligomeric state. However, the compositions of the vast majority are unknown. This paper describes a biochemical method to predict protein complex composition based on orthogonal chromatographic separations and label-free protein correlation profiling. The validated method predicts hundreds of novel homo- and heterooligomeric complexes, and provides a new way to analyze protein complexes in any organism with a well-annotated proteome.

  • Unraveling Hidden Components of the Chloroplast Envelope Proteome: Opportunities and Limits of Better MS Sensitivity
    Open Access
    Unraveling Hidden Components of the Chloroplast Envelope Proteome: Opportunities and Limits of Better MS Sensitivity
    Imen Bouchnak, Sabine Brugière, Lucas Moyet, Sophie Le Gall, Daniel Salvi, Marcel Kuntz, Marianne Tardif and Norbert Rolland
    Molecular & Cellular Proteomics July 1, 2019, First published on April 8, 2019, 18 (7) 1285-1306; https://doi.org/10.1074/mcp.RA118.000988

    By quantitatively comparing the proteomes of total leaf (crude cell extract) from Arabidopsis and purified chloroplast envelope fractions, this study makes available a novel parameter (calculated Enrichment Factor) for each putative envelope protein. This parameter provides important information to enable the more confident identification of genuine envelope components, distinguishing them from contaminants from other cellular/chloroplast compartments.

  • Complexome Profiling Reveals Association of PPR Proteins with Ribosomes in the Mitochondria of Plants
    You have access
    Complexome Profiling Reveals Association of PPR Proteins with Ribosomes in the Mitochondria of Plants
    Nils Rugen, Henryk Straube, Linda E. Franken, Hans-Peter Braun and Holger Eubel
    Molecular & Cellular Proteomics July 1, 2019, First published on April 25, 2019, 18 (7) 1345-1362; https://doi.org/10.1074/mcp.RA119.001396

    Plant mitochondrial protein expression is complex and routinely involves pentatricopeptide repeat proteins for processing of transcripts. Although the composition and structure of the mitoribosomes in other eukaryotic kingdoms of life is well established, plant mitochondria have so far eluded a detailed analysis. Using a complexome profiling approach, this study provides an early glimpse on the composition of plant mitochondrial ribosomes and sheds new light on the process of mitochondrial gene expression in plants. Mitochondrial subunits were found to possess several additional proteins carrying pentatricopeptide repeats potentially involved in RNA editing. Other proteins are potentially involved in the processing of nascent proteins.

  • Quantitative Early Auxin Root Proteomics Identifies GAUT10, a Galacturonosyltransferase, as a Novel Regulator of Root Meristem Maintenance
    Open Access
    Quantitative Early Auxin Root Proteomics Identifies GAUT10, a Galacturonosyltransferase, as a Novel Regulator of Root Meristem Maintenance
    Yunting Pu, Justin W. Walley, Zhouxin Shen, Michelle G. Lang, Steven P. Briggs, Mark Estelle and Dior R. Kelley
    Molecular & Cellular Proteomics June 1, 2019, First published on March 27, 2019, 18 (6) 1157-1170; https://doi.org/10.1074/mcp.RA119.001378

    Auxin induces rapid abundance changes in various signaling proteins, transcriptional regulators, and enzymes such as cell wall modification proteins in roots. Loss of function of 15 top responsive proteins results in altered root phenotypes, demonstrating the power of this approach for reverse genetics screens. Characterization of the auxin responsive protein galacturonosyltransferase 10 demonstrates that this enzyme positively regulates sugar-mediated root meristem maintenance. Novel targeted proteomics assays demonstrate that all six auxin receptors remain stable in response to hormone.

  • You have access
    Integrated Transcriptomic and Proteomic Analyses Suggest the Participation of Endogenous Protease Inhibitors in the Regulation of Protease Gene Expression in Helicoverpa armigera
    Purushottam R. Lomate, Veena Dewangan, Neha S. Mahajan, Yashwant Kumar, Abhijeet Kulkarni, Li Wang, Smita Saxena, Vidya S. Gupta and Ashok P. Giri
    Molecular & Cellular Proteomics July 1, 2018, First published on April 16, 2018, 17 (7) 1324-1336; https://doi.org/10.1074/mcp.RA117.000533
  • You have access
    Protease Activities Triggered by Ralstonia solanacearum Infection in Susceptible and Tolerant Tomato Lines
    Marc Planas-Marquès, Martí Bernardo-Faura, Judith Paulus, Farnusch Kaschani, Markus Kaiser, Marc Valls, Renier A. L. van der Hoorn and Núria S. Coll
    Molecular & Cellular Proteomics June 1, 2018, First published on March 9, 2018, 17 (6) 1112-1125; https://doi.org/10.1074/mcp.RA117.000052

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