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dc.contributor.authorBarr, Zoe Kathleen
dc.contributor.authorWerner, Tomáš
dc.contributor.authorTilsner, Jens
dc.date.accessioned2023-08-24T14:30:09Z
dc.date.available2023-08-24T14:30:09Z
dc.date.issued2023-08-21
dc.identifier292411404
dc.identifier57ab4d1e-9e11-4602-b372-76763f92d5df
dc.identifier85169074970
dc.identifier.citationBarr , Z K , Werner , T & Tilsner , J 2023 , ' Heavy metal-associated isoprenylated plant proteins (HIPPs) at plasmodesmata : exploring the link between localization and function ' , Plants , vol. 12 , no. 16 , 3015 . https://doi.org/10.3390/plants12163015en
dc.identifier.issn2223-7747
dc.identifier.urihttps://hdl.handle.net/10023/28229
dc.descriptionFunding: This work was supported by the U.K. Biotechnology and Biological Sciences Research Council (BBSRC) through an Eastbio Doctoral Training Partnership scholarship to Z.B, and by the Austrian Science Fund grant P 30945 to T.W. Work in the J.T. laboratory is supported by the Scottish Government’s Rural and Environment Science and Analytical Services Division (RESAS).en
dc.description.abstractHeavy 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.
dc.format.extent15
dc.format.extent956435
dc.language.isoeng
dc.relation.ispartofPlantsen
dc.subjectPlasmodesmataen
dc.subjectHeavy metal-associated plant proteinsen
dc.subjectHIPPen
dc.subjectPrenylationen
dc.subjectMetallochaperoneen
dc.subjectAbiotic and biotic stressen
dc.subjectCytokininen
dc.subjectQH301 Biologyen
dc.subjectSB Plant cultureen
dc.subjectMCCen
dc.subject.lccQH301en
dc.subject.lccSBen
dc.titleHeavy metal-associated isoprenylated plant proteins (HIPPs) at plasmodesmata : exploring the link between localization and functionen
dc.typeJournal itemen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Centre for Biophotonicsen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doi10.3390/plants12163015
dc.description.statusPeer revieweden
dc.identifier.urlhttps://www.mdpi.com/journal/plants/special_issues/2M2344JFP6en


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