Heavy metal-associated isoprenylated plant proteins (HIPPs) at plasmodesmata: exploring the link between localization and function

Zoe Kathleen Barr, Tomáš Werner*, Jens Tilsner*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

2 Citations (Scopus)
6 Downloads (Pure)

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.
Original languageEnglish
Article number3015
Number of pages15
JournalPlants
Volume12
Issue number16
DOIs
Publication statusPublished - 21 Aug 2023

Keywords

  • Plasmodesmata
  • Heavy metal-associated plant proteins
  • HIPP
  • Prenylation
  • Metallochaperone
  • Abiotic and biotic stress
  • Cytokinin

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