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Plant VAP 27 proteins: domain characterization, intracellular localization and role in plant development
Author(s) -
Wang Pengwei,
Richardson Christine,
Hawkins Timothy J.,
Sparkes Imogen,
Hawes Chris,
Hussey Patrick J.
Publication year - 2016
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.13857
Subject(s) - arabidopsis , biology , microbiology and biotechnology , plasmodesma , nicotiana benthamiana , endoplasmic reticulum , cytoskeleton , actin cytoskeleton , gene , genetics , cell , mutant , cytoplasm
Summary The endoplasmic reticulum ( ER ) is connected to the plasma membrane ( PM ) through the plant‐specific NETWORKED protein, NET 3C, and phylogenetically conserved vesicle‐associated membrane protein‐associated proteins ( VAP s). Ten VAP homologues ( VAP 27‐1 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 ( EPCS s), whereas proteins from clade II were found only at the PM . Some of the VAP 27‐labelled EPCS s localized to plasmodesmata, and we show that the mobility of VAP 27 at EPCS s is influenced by the cell wall. EPCS s closely associate with the cytoskeleton, but their structure is unaffected when the cytoskeleton is removed. VAP 27‐labelled EPCS s are found in most cell types in Arabidopsis, with the exception of cells in early trichome development. Arabidopsis plants expressing VAP 27‐ GFP fusions exhibit pleiotropic phenotypes, including defects in root hair morphogenesis. A similar effect is also observed in plants expressing VAP 27 RNA i. Taken together, these data indicate that VAP 27 proteins used at EPCS s are essential for normal ER –cytoskeleton interaction and for plant development.