A specific role for Arabidopsis TRAPPII in post-Golgi trafficking that is crucial for cytokinesis and cell polarity

Authors

  • Xingyun Qi,

    1. Developmental Biology Research Initiatives, Department of Biology, McGill University, 1205 Dr Penfield Avenue, Montreal, Quebec H3A 1B1, Canada
    Search for more papers by this author
  • Minako Kaneda,

    1. Department of Biological Sciences, Institut de recherche en biologie végétale, University of Montreal, 4101 Sherbrooke east, Montreal, Quebec H1X 2B2, Canada
    Search for more papers by this author
  • Jun Chen,

    1. Developmental Biology Research Initiatives, Department of Biology, McGill University, 1205 Dr Penfield Avenue, Montreal, Quebec H3A 1B1, Canada
    Search for more papers by this author
  • Anja Geitmann,

    1. Department of Biological Sciences, Institut de recherche en biologie végétale, University of Montreal, 4101 Sherbrooke east, Montreal, Quebec H1X 2B2, Canada
    Search for more papers by this author
  • Huanquan Zheng

    Corresponding author
    1. Developmental Biology Research Initiatives, Department of Biology, McGill University, 1205 Dr Penfield Avenue, Montreal, Quebec H3A 1B1, Canada
    Search for more papers by this author

(fax +1 514 398 5069; e-mail hugo.zheng@mcgill.ca).

Summary

Cytokinesis and cell polarity are supported by membrane trafficking from the trans-Golgi network (TGN), but the molecular mechanisms that promote membrane trafficking from the TGN are poorly defined in plant cells. Here we show that TRAPPII in Arabidopsis regulates the post-Golgi trafficking that is crucial for assembly of the cell plate and cell polarity. Disruptions of AtTRS120 or AtTRS130, two genes encoding two key subunits of TRAPPII, result in defective cytokinesis and cell polarity in embryogenesis and seedling development. In attrs120 and attrs130, the organization and trafficking in the endoplasmic reticulum (ER)–Golgi interface are normal. However, post-Golgi trafficking to the cell plate and to the cell wall, but not to the vacuole, is impaired. Furthermore, TRAPPII is required for the selective transport of PIN2, but not PIN1, to the plasma membrane. We revealed that AtTRS130 is co-localized with RAB-A1c. Expression of constitutively active RAB-A1c partially rescues attrs130. RAB-A1c, which resides at the TGN, is delocalized to the cytosol in attrs130. We propose that TRAPPII in Arabidopsis acts upstream of Rab-A GTPases in post-Golgi membrane trafficking in plant cells.

Ancillary