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Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus
Author(s) -
Yeats Trevor H.,
Bacic Antony,
Johnson Kim L.
Publication year - 2018
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12659
Subject(s) - biology , proteome , microbiology and biotechnology , arabidopsis , signal transduction , cell wall , arabinogalactan , membrane protein , context (archaeology) , protein targeting , biochemistry , mutant , membrane , gene , paleontology
Approximately 1% of plant proteins are predicted to be post‐translationally modified with a glycosylphosphatidylinositol (GPI) anchor that tethers the polypeptide to the outer leaflet of the plasma membrane. Whereas the synthesis and structure of GPI anchors is largely conserved across eukaryotes, the repertoire of functional domains present in the GPI‐anchored proteome has diverged substantially. In plants, this includes a large fraction of the GPI‐anchored proteome being further modified with plant‐specific arabinogalactan (AG) O‐ glycans. The importance of the GPI‐anchored proteome to plant development is underscored by the fact that GPI biosynthetic null mutants exhibit embryo lethality. Mutations in genes encoding specific GPI‐anchored proteins (GAPs) further supports their contribution to diverse biological processes, occurring at the interface of the plasma membrane and cell wall, including signaling, cell wall metabolism, cell wall polymer cross‐linking, and plasmodesmatal transport. Here, we review the literature concerning plant GPI‐anchored proteins, in the context of their potential to act as molecular hubs that mediate interactions between the plasma membrane and the cell wall, and their potential to transduce the signal into the protoplast and, thereby, activate signal transduction pathways.