4.8 Article

TRIPP Is a Plant-Specific Component of the Arabidopsis TRAPPII Membrane Trafficking Complex with Important Roles in Plant Development

期刊

PLANT CELL
卷 32, 期 7, 页码 2424-2443

出版社

OXFORD UNIV PRESS INC
DOI: 10.1105/tpc.20.00044

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资金

  1. National Institute Of General Medical Sciences of the National Institutes of Health [R01GM066258]
  2. Carnegie Endowment Fund
  3. Deutsche Forschungsgemeinschaft (DFG) [AS110/4-7, AS110/5-2, SFB 924/2-A10]
  4. Leverhulme Trust [RPG-2014-2761]
  5. European Research Council [648420]
  6. Biotechnology and Biological Sciences Research Council [1810136]
  7. BBSRC [1810136] Funding Source: UKRI
  8. European Research Council (ERC) [648420] Funding Source: European Research Council (ERC)

向作者/读者索取更多资源

A proteomic study sheds light on Transport Protein Particle (TRAPP) proteins in plants and identifies TRIPP as a plant-specific component of the TRAPPII complex with important roles in vesicle trafficking and plant development. How the membrane trafficking system spatially organizes intracellular activities and intercellular signaling networks in plants is not well understood. Transport Protein Particle (TRAPP) complexes play key roles in the selective delivery of membrane vesicles to various subcellular compartments in yeast and animals but remain to be fully characterized in plants. Here, we investigated TRAPP complexes in Arabidopsis (Arabidopsis thaliana) using immunoprecipitation followed by quantitative mass spectrometry analysis of AtTRS33, a conserved core component of all TRAPP complexes. We identified 14 AtTRS33-interacting proteins, including homologs of all 13 TRAPP components in mammals and a protein that has homologs only in multicellular photosynthetic organisms and is thus named TRAPP-Interacting Plant Protein (TRIPP). TRIPP specifically associates with the TRAPPII complex through binary interactions with two TRAPPII-specific subunits. TRIPP colocalized with a subset of TRS33 compartments and trans-Golgi network markers in a TRS33-dependent manner. Loss-of-function tripp mutants exhibited dwarfism, sterility, partial photomorphogenesis in the dark, reduced polarity of the auxin transporter PIN2, incomplete cross wall formation, and altered localization of a TRAPPII-specific component. Therefore, TRIPP is a plant-specific component of the TRAPPII complex with important functions in trafficking, plant growth, and development.

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