Plant VAP27 proteins: domain characterization, intracellular localization and role in plant development

Pengwei Wang, Christine Richardson, Timothy J Hawkins, Imogen Sparkes, Chris Hawes, Patrick J Hussey

Research output: Contribution to journalArticle (Academic Journal)peer-review

89 Citations (Scopus)
317 Downloads (Pure)


The endoplasmic reticulum (ER) is connected to the plasma membrane (PM) through the plant-specific NETWORKED protein, NET3C, and phylogenetically conserved vesicle-associated membrane protein-associated proteins (VAPs). Ten VAP homologues (VAP27-1 to 27-10) can be identified in the Arabidopsis genome and can be divided into three clades. Representative members from each clade were tagged with fluorescent protein and expressed in Nicotiana benthamiana. Proteins from clades I and III localized to the ER as well as to ER/PM contact sites (EPCSs), whereas proteins from clade II were found only at the PM. Some of the VAP27-labelled EPCSs localized to plasmodesmata, and we show that the mobility of VAP27 at EPCSs is influenced by the cell wall. EPCSs closely associate with the cytoskeleton, but their structure is unaffected when the cytoskeleton is removed. VAP27-labelled EPCSs are found in most cell types in Arabidopsis, with the exception of cells in early trichome development. Arabidopsis plants expressing VAP27-GFP fusions exhibit pleiotropic phenotypes, including defects in root hair morphogenesis. A similar effect is also observed in plants expressing VAP27 RNAi. Taken together, these data indicate that VAP27 proteins used at EPCSs are essential for normal ER-cytoskeleton interaction and for plant development.

Original languageEnglish
Pages (from-to)1311-1326
Number of pages16
JournalNew Phytologist
Issue number4
Early online date1 Feb 2016
Publication statusPublished - 9 May 2016


  • Journal Article


Dive into the research topics of 'Plant VAP27 proteins: domain characterization, intracellular localization and role in plant development'. Together they form a unique fingerprint.

Cite this