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Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome

Hundreds of candidate 14-3-3-binding (phospho)proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from lo...

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Autores principales: Johnson, Catherine, Tinti, Michele, Wood, Nicola T., Campbell, David G., Toth, Rachel, Dubois, Fanny, Geraghty, Kathryn M., Wong, Barry H. C., Brown, Laura J., Tyler, Jennifer, Gernez, Aurélie, Chen, Shuai, Synowsky, Silvia, MacKintosh, Carol
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Biochemistry and Molecular Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205853/
https://www.ncbi.nlm.nih.gov/pubmed/21725060
http://dx.doi.org/10.1074/mcp.M110.005751
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author Johnson, Catherine
Tinti, Michele
Wood, Nicola T.
Campbell, David G.
Toth, Rachel
Dubois, Fanny
Geraghty, Kathryn M.
Wong, Barry H. C.
Brown, Laura J.
Tyler, Jennifer
Gernez, Aurélie
Chen, Shuai
Synowsky, Silvia
MacKintosh, Carol
author_facet Johnson, Catherine
Tinti, Michele
Wood, Nicola T.
Campbell, David G.
Toth, Rachel
Dubois, Fanny
Geraghty, Kathryn M.
Wong, Barry H. C.
Brown, Laura J.
Tyler, Jennifer
Gernez, Aurélie
Chen, Shuai
Synowsky, Silvia
MacKintosh, Carol
author_sort Johnson, Catherine
collection PubMed
description Hundreds of candidate 14-3-3-binding (phospho)proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from low-throughput studies in MINT (http://mint.bio.uniroma2.it/mint), and compared the low- and high-throughput data in VisANT graphs that are easy to analyze and extend. Exploring the graphs prompted questions about technical and biological specificity, which were addressed experimentally, resulting in identification of phosphorylated 14-3-3-binding sites in the mitochondrial import sequence of the iron-sulfur cluster assembly enzyme (ISCU), cytoplasmic domains of the mitochondrial fission factor (MFF), and endoplasmic reticulum-tethered receptor expression-enhancing protein 4 (REEP4), RNA regulator SMAUG2, and cytoskeletal regulatory proteins, namely debrin-like protein (DBNL) and kinesin light chain (KLC) isoforms. Therefore, 14-3-3s undergo physiological interactions with proteins that are destined for diverse subcellular locations. Graphing and validating interactions underpins efforts to use 14-3-3-phosphoproteomics to identify mechanisms and biomarkers for signaling pathways in health and disease.
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spelling pubmed-32058532011-11-14 Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome Johnson, Catherine Tinti, Michele Wood, Nicola T. Campbell, David G. Toth, Rachel Dubois, Fanny Geraghty, Kathryn M. Wong, Barry H. C. Brown, Laura J. Tyler, Jennifer Gernez, Aurélie Chen, Shuai Synowsky, Silvia MacKintosh, Carol Mol Cell Proteomics Research Hundreds of candidate 14-3-3-binding (phospho)proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from low-throughput studies in MINT (http://mint.bio.uniroma2.it/mint), and compared the low- and high-throughput data in VisANT graphs that are easy to analyze and extend. Exploring the graphs prompted questions about technical and biological specificity, which were addressed experimentally, resulting in identification of phosphorylated 14-3-3-binding sites in the mitochondrial import sequence of the iron-sulfur cluster assembly enzyme (ISCU), cytoplasmic domains of the mitochondrial fission factor (MFF), and endoplasmic reticulum-tethered receptor expression-enhancing protein 4 (REEP4), RNA regulator SMAUG2, and cytoskeletal regulatory proteins, namely debrin-like protein (DBNL) and kinesin light chain (KLC) isoforms. Therefore, 14-3-3s undergo physiological interactions with proteins that are destined for diverse subcellular locations. Graphing and validating interactions underpins efforts to use 14-3-3-phosphoproteomics to identify mechanisms and biomarkers for signaling pathways in health and disease. The American Society for Biochemistry and Molecular Biology 2011-10 2011-07-01 /pmc/articles/PMC3205853/ /pubmed/21725060 http://dx.doi.org/10.1074/mcp.M110.005751 Text en © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Research
Johnson, Catherine
Tinti, Michele
Wood, Nicola T.
Campbell, David G.
Toth, Rachel
Dubois, Fanny
Geraghty, Kathryn M.
Wong, Barry H. C.
Brown, Laura J.
Tyler, Jennifer
Gernez, Aurélie
Chen, Shuai
Synowsky, Silvia
MacKintosh, Carol
Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title_full Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title_fullStr Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title_full_unstemmed Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title_short Visualization and Biochemical Analyses of the Emerging Mammalian 14-3-3-Phosphoproteome
title_sort visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3205853/
https://www.ncbi.nlm.nih.gov/pubmed/21725060
http://dx.doi.org/10.1074/mcp.M110.005751
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