Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function
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 pro...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-08-01
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| Series: | Plants |
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| Online Access: | https://www.mdpi.com/2223-7747/12/16/3015 |
| _version_ | 1797583406789296128 |
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| author | Zoe Kathleen Barr Tomáš Werner Jens Tilsner |
| author_facet | Zoe Kathleen Barr Tomáš Werner Jens Tilsner |
| author_sort | Zoe Kathleen Barr |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T23:38:29Z |
| format | Article |
| id | doaj.art-462bd081c2e846858ecb0812982ed545 |
| institution | Directory Open Access Journal |
| issn | 2223-7747 |
| language | English |
| last_indexed | 2024-03-10T23:38:29Z |
| publishDate | 2023-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Plants |
| spelling | doaj.art-462bd081c2e846858ecb0812982ed5452023-11-19T02:42:29ZengMDPI AGPlants2223-77472023-08-011216301510.3390/plants12163015Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and FunctionZoe Kathleen Barr0Tomáš Werner1Jens Tilsner2Biomedical Sciences Research Complex, University of St Andrews, BMS Building, North Haugh, St Andrews, Fife KY16 9ST, UKDepartment of Biology, University of Graz, Schubertstraße 51, 8010 Graz, AustriaBiomedical Sciences Research Complex, University of St Andrews, BMS Building, North Haugh, St Andrews, Fife KY16 9ST, UKHeavy 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.https://www.mdpi.com/2223-7747/12/16/3015plasmodesmataheavy metal-associated plant proteinsHIPPprenylationmetallochaperoneabiotic and biotic stress |
| spellingShingle | Zoe Kathleen Barr Tomáš Werner Jens Tilsner Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function Plants plasmodesmata heavy metal-associated plant proteins HIPP prenylation metallochaperone abiotic and biotic stress |
| title | Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function |
| title_full | Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function |
| title_fullStr | Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function |
| title_full_unstemmed | Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function |
| title_short | Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization and Function |
| title_sort | heavy metal associated isoprenylated plant proteins hipps at plasmodesmata exploring the link between localization and function |
| topic | plasmodesmata heavy metal-associated plant proteins HIPP prenylation metallochaperone abiotic and biotic stress |
| url | https://www.mdpi.com/2223-7747/12/16/3015 |
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