VAPYRIN-like is required for development of the moss Physcomitrella patens

Abstract

The VAPYRIN (VPY) gene in Medicago truncatula and Petunia hybrida is required for arbuscular mycorrhizal (AM) symbiosis. The moss Physcomitrella patens has a close homologue (VPY-like, VPYL), although it does not form AM. Here, we explore the phylogeny of VPY and VPYL in land plants, and we study the expression and developmental function of VPYL in P. patens. We show that PpVPYL is expressed primarily in the protonema, the early filamentous stage of moss development, and later in rhizoids arising from the leafy gametophores and in adult phyllids. Knockout mutants have specific phenotypes in branching of the protonema and in cell division of the leaves (phyllids) in gametophores. The mutants are responsive to auxin and strigolactone, which are involved in the regulation of protonemal branching, indicating that the mutants are not affected in hormonal signaling. Taken together, these results suggest that PpVPYL exerts negative regulation of protonemal branching and of cell division in phyllids. We discuss VPY and VPYL phylogeny and function in land plants in the context of AM symbiosis in angiosperms, and of development in the moss.

A cornichon protein controls polar localization of the PINA auxin transporter inPhyscomitrium patens

“…We observed abnormal positioning of branching cells in the cornichon mutants (Figure 2A-B and Supplemental Figure S4). Until now, it has only been reported that mutants in Myosin VIII (Wu et al, 2011) and a Vapyrin-like (VPY-like) protein (Rathgeb et al, 2020) exhibit these branching defects. In moss protonemata, one of this cornichon-interacting proteins could be a VPY-like protein according to its localization to puncta in the cytoplasm and around the nucleus, coincident to that we observed for CNIH2 (Figure 5A).…”

“…In moss protonemata, one of this cornichon-interacting proteins could be a VPY-like protein according to its localization to puncta in the cytoplasm and around the nucleus, coincident to that we observed for CNIH2 (Figure 5A). The localization of VPY and VPY-like proteins was denoted as vapyrin bodies related to the TGN and endosomes, but also associated with the endoplasmic reticulum (Pumplin et al, 2010; Feddermann et al, 2010; Liu et al, 2019; Bapaume et al, 2019; Rathgeb et al, 2020). Although the function of Vapyrin (VPY) and VPY-like proteins is unknown, they are only found in plants and possess a vesicle-associated protein (VAP) domain at their N-terminus, and several ankyrin repeat domains at the C-terminus, with both domains predicted to be involved in protein-protein interactions (Pumplin et al, 2010; Feddermann et al, 2010), opening the possibility that they could associate with CNIH2.…”

Plant evolution driven by interactions with symbiotic and pathogenic microbes

“…This is illustrated by VAPYRIN and VPY-like, two genes originating from an embryophyte-specific gene duplication. In angiosperm both genes are co-eliminated with the loss of AM symbiosis while they are, one or the other, maintained in Bryophytes irrespective of their symbiotic abilities (57,65). In the moss P. patens, inactivation of VPY-like, the paralog maintained in mosses, results in developmental defects in the gametophyte (65).…”

Multilevel analysis between Physcomitrium patens and Mortierellaceae endophytes explores potential long‐standing interaction among land plants and fungi

“…Additionally, evidence that P. patens has (or had) the capacity for interacting with fungi can be supported by the presence of orthologs essential to detecting and forming plant–fungal interaction. Some conserved genes that are indicative of this possibility include a chitin‐like receptor PpCERK1 necessary to signal the environmental presence of fungi, a VAPYRIN ‐like homolog with only known function in forming symbiotic interaction between plants and fungi, and functional strigolactone hormone pathways with secondary functions known to signal host root proximity to symbiotic and parasitic fungi (Bressendorff et al., 2016; Delaux & Schornack, 2021; Proust et al., 2011; Rathgeb et al., 2020).…”