Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function

Author:

Barr Zoe Kathleen12ORCID,Werner Tomáš3ORCID,Tilsner Jens12ORCID

Affiliation:

1. Biomedical Sciences Research Complex, University of St Andrews, BMS Building, North Haugh, St Andrews, Fife KY16 9ST, UK

2. Cell & Molecular Sciences, The James Hutton Institute, Dundee DD2 5DA, UK

3. Department of Biology, University of Graz, Schubertstraße 51, 8010 Graz, Austria

Abstract

Heavy metal-associated isoprenylated plant proteins (HIPPs) are a metallochaperone-like protein family comprising a combination of structural features unique to vascular plants. HIPPs possess both one or two heavy metal-binding domains and an isoprenylation site, facilitating a posttranslational protein lipid modification. Recent work has characterized individual HIPPs across numerous different species and provided evidence for varied functionalities. Interestingly, a significant number of HIPPs have been identified in proteomes of plasmodesmata (PD)—nanochannels mediating symplastic connectivity within plant tissues that play pivotal roles in intercellular communication during plant development as well as responses to biotic and abiotic stress. As characterized functions of many HIPPs are linked to stress responses, plasmodesmal HIPP proteins are potentially interesting candidate components of signaling events at or for the regulation of PD. Here, we review what is known about PD-localized HIPP proteins specifically, and how the structure and function of HIPPs more generally could link to known properties and regulation of PD.

Funder

Biotechnology and Biological Sciences Research Council

FWF Austrian Science Fund

Publisher

MDPI AG

Subject

Plant Science,Ecology,Ecology, Evolution, Behavior and Systematics

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