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Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development

View ORCID ProfileVeder J. Garcia, View ORCID ProfileShou-Ling Xu, Raksha Ravikumar, View ORCID ProfileWenfei Wang, Liam Elliott, Mary Fesenko, Melina Altmann, Pascal Falter-Braun, Ian Moore, Farhah F. Assaad, Zhi-Yong Wang
doi: https://doi.org/10.1101/684258
Veder J. Garcia
1Department of Plant Biology, Carnegie Institution for Science, Stanford, CA, 94305
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Shou-Ling Xu
1Department of Plant Biology, Carnegie Institution for Science, Stanford, CA, 94305
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Raksha Ravikumar
2Plant Science Department, Botany, Technische Universität München, 85354 Freising, Germany
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Wenfei Wang
3Basic Forestry and Proteomics Research Center, Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University, Fuzhou, China
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Liam Elliott
4Department of Plant Sciences, South Parks Road, Oxford, OX1 3RB, UK
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Mary Fesenko
4Department of Plant Sciences, South Parks Road, Oxford, OX1 3RB, UK
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Melina Altmann
5Institute of Network Biology (INET), Helmholtz Zentrum München, Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH), 85764 Neuherberg, Germany
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Pascal Falter-Braun
5Institute of Network Biology (INET), Helmholtz Zentrum München, Deutsches Forschungszentrum für Gesundheit und Umwelt (GmbH), 85764 Neuherberg, Germany
6Faculty of Biology, Microbe-Host-Interactions, Ludwig-Maximilians-Universität (LMU) München, 82152 Planegg-Martinsried, Germany
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Ian Moore
4Department of Plant Sciences, South Parks Road, Oxford, OX1 3RB, UK
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Farhah F. Assaad
2Plant Science Department, Botany, Technische Universität München, 85354 Freising, Germany
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Zhi-Yong Wang
1Department of Plant Biology, Carnegie Institution for Science, Stanford, CA, 94305
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  • For correspondence: zywang24@stanford.edu
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Abstract

How the membrane trafficking system spatially organizes intracellular activities and intercellular signaling networks is not well understood in plants. The Transport Protein Particle (TRAPP) complexes are known to play key roles in selective delivery of membrane vesicles to various subcellular compartments in yeast and animals, but remain to be fully characterized in plants. Here we interrogate the TRAPP complexes in Arabidopsis using quantitative proteomic approaches. TRS33 is a component shared by all TRAPP complexes in yeast and animals, and the Arabidopsis AtTRS33 is essential for the subcellular dynamics of other TRAPP components. Affinity purification of AtTRS33 followed by quantitative mass spectrometry identified fourteen interacting proteins; these include not only thirteen homologs of all known TRAPP components in yeast and mammals but also a novel protein we named TRAPP-interacting plant protein (TRIPP), which is conserved in multi-cellular photosynthetic organisms. Proteomic and molecular analyses showed that TRIPP specifically associates with the TRAPPII complex in vivo and directly interacts with the TRAPPII-specific subunits but not the subunits shared with TRAPPIII. TRIPP co-localizes with a subset of TRS33 compartments, and its localization is disrupted in the trs33 mutant. Loss-of-function tripp mutation caused growth and reproductive development defects, including partial photomorphogenesis in the dark. Our study demonstrates that plants possess at least two distinct TRAPP complexes similar to metazoan, and identifies TRIPP as a novel plant-specific component of the TRAPPII complex with important functions in plant growth and development.

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Posted June 28, 2019.
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Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development
Veder J. Garcia, Shou-Ling Xu, Raksha Ravikumar, Wenfei Wang, Liam Elliott, Mary Fesenko, Melina Altmann, Pascal Falter-Braun, Ian Moore, Farhah F. Assaad, Zhi-Yong Wang
bioRxiv 684258; doi: https://doi.org/10.1101/684258
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Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development
Veder J. Garcia, Shou-Ling Xu, Raksha Ravikumar, Wenfei Wang, Liam Elliott, Mary Fesenko, Melina Altmann, Pascal Falter-Braun, Ian Moore, Farhah F. Assaad, Zhi-Yong Wang
bioRxiv 684258; doi: https://doi.org/10.1101/684258

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