The Key to Mn Homeostasis in Plants: Regulation of Mn Transporters

Shao, Ji Feng; Yamaji, Naoki; Shen, Ren Fang; Feng, Jian

doi:10.1016/j.tplants.2016.12.005

Cited by 157 publications

(92 citation statements)

References 49 publications

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“…For instance, Cd is mainly sequestered in vacuoles of parenchyma cells in the leaf mesophyll, stem pith, and cortex in the shoots of the Zn/Cd hyperaccumulator S. alfredii (Tian et al, 2017) identifying and functionally characterizing the transporters for these essential metal ions has helped to elucidate the transporters involved in the uptake and translocation of nonessential and toxic HM ions. The roles of many transporters in HM absorption and transport have been characterized in model plants and some hyperaccumulators (Migeon et al, 2010;Shao et al, 2017). These HM transporters include members of the zinc-iron permease (ZIP) family, the natural resistanceassociated macrophage protein (NRAMP) family, and the heavy metal ATPases (HMA) family.…”

Section: Lópezmentioning

confidence: 99%

“…In recent years, great progress has been made in our understanding of the physiological and molecular mechanisms that underlie the uptake, translocation, detoxification, and accumulation of HMs in nonmycorrhizal plants (Clemens & Ma, 2016;Fasani, Manara, Martini, Furini, & Dalcorso, 2018;Luo, He, Polle, & Rennenberg, 2016;Shao, Yamaji, Shen, & Ma, 2017), as well as in mycorrhizal plants (Ho-Man et al, 2013;Luo et al, 2014). In this review, we first describe recent 2.1 | Physiological mechanisms underlying HM accumulation 2.1.1 | Uptake and transport of HMs via apoplastic and symplastic pathways HM ions in the soil solution move according to their respective concentration gradients.…”

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confidence: 99%

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Physiological and molecular mechanisms of heavy metal accumulation in nonmycorrhizal versus mycorrhizal plants

Shi

Zhang

Chen

et al. 2018

Plant Cell & Environment

138

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Uptake, translocation, detoxification, and sequestration of heavy metals (HMs) are key processes in plants to deal with excess amounts of HM. Under natural conditions, plant roots often establish ecto‐ and/or arbuscular‐mycorrhizae with their fungal partners, thereby altering HM accumulation in host plants. This review considers the progress in understanding the physiological and molecular mechanisms involved in HM accumulation in nonmycorrhizal versus mycorrhizal plants. In nonmycorrhizal plants, HM ions in the cells can be detoxified with the aid of several chelators. Furthermore, HMs can be sequestered in cell walls, vacuoles, and the Golgi apparatus of plants. The uptake and translocation of HMs are mediated by members of ZIPs, NRAMPs, and HMAs, and HM detoxification and sequestration are mainly modulated by members of ABCs and MTPs in nonmycorrhizal plants. Mycorrhizal‐induced changes in HM accumulation in plants are mainly due to HM sequestration by fungal partners and improvements in the nutritional and antioxidative status of host plants. Furthermore, mycorrhizal fungi can trigger the differential expression of genes involved in HM accumulation in both partners. Understanding the molecular mechanisms that underlie HM accumulation in mycorrhizal plants is crucial for the utilization of fungi and their host plants to remediate HM‐contaminated soils.

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Section: Lópezmentioning

confidence: 99%

mentioning

confidence: 99%

Physiological and molecular mechanisms of heavy metal accumulation in nonmycorrhizal versus mycorrhizal plants

Shi

Zhang

Chen

et al. 2018

Plant Cell & Environment

138

View full text Add to dashboard Cite

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“…This cooperative system ensures root B uptake, B rootto-shoot translocation and B loading into specific cells, tissues or the apoplast of different model and crop plant species (Takano et al, 2006;Miwa et al, 2007;Reid, 2007;Sutton et al, 2007;Tanaka et al, 2008;Kajikawa et al, 2011;Miwa et al, 2013;Chatterjee et al, 2014Chatterjee et al, , 2017Durbak et al, 2014;Hanaoka et al, 2014;Pallotta et al, 2014;Hua et al, 2016a;Routray et al, 2018;Shao et al, 2018). Additionally, BORs and NIPs have been demonstrated to be decisive factors determining plant B toxicity tolerance (Miwa and Fujiwara, 2010).…”

Section: Introductionmentioning

confidence: 99%

Boron demanding tissues of Brassica napus express specific sets of functional Nodulin26‐like Intrinsic Proteins and BOR1 transporters

et al. 2019

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SummaryThe sophisticated uptake and translocation regulation of the essential element boron (B) in plants is ensured by two transmembrane transporter families: the Nodulin26‐like Intrinsic Protein (NIP) and BOR transporter family. Though the agriculturally important crop Brassica napus is highly sensitive to B deficiency, and NIPs and BORs have been suggested to be responsible for B efficiency in this species, functional information of these transporter subfamilies is extremely rare. Here, we molecularly characterized the NIP and BOR1 transporter family in the European winter‐type cv. Darmor‐PBY018. Our transport assays in the heterologous oocyte and yeast expression systems as well as in growth complementation assays in planta demonstrated B transport activity of NIP5, NIP6, NIP7 and BOR1 isoforms. Moreover, we provided functional and quantitative evidence that also members of the NIP2, NIP3 and NIP4 groups facilitate the transport of B. A detailed B‐ and tissue‐dependent B‐transporter expression map was generated by quantitative polymerase chain reaction. We showed that NIP5 isoforms are highly upregulated under B‐deficient conditions in roots, but also in shoot tissues. Moreover, we detected transcripts of several B‐permeable NIPs from various groups in floral tissues that contribute to the B distribution within the highly B deficiency‐sensitive flowers.

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“…Moreover, Arabidopsis does not have Si channel homologous to rice Lsi1 in the genome . This regulation mechanism is similar to that for Mn in rice (Yamaji et al, 2013;Shao et al, 2017). OsNramp3 in the node required for Mn distribution, rather than OsNramp5 and OsMTP9 in the roots for Mn uptake, is regulated at the protein level in response to environmental Mn change (Shao et al, 2017).…”

Section: Different Regulation Of B Accumulation In Rice and Arabidopsismentioning

confidence: 75%

Preferential Distribution of Boron to Developing Tissues Is Mediated by the Intrinsic Protein OsNIP3

et al. 2017

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Boron is especially required for the growth of meristem and reproductive organs, but the molecular mechanisms underlying the preferential distribution of B to these developing tissues are poorly understood. Here, we show evidence that a member of nodulin 26-like intrinsic protein (NIP), OsNIP3;1, is involved in this preferential distribution in rice (Oryza sativa). OsNIP3;1 was highly expressed in the nodes and its expression was up-regulated by B deficiency, but down-regulated by high B. OsNIP3;1 was polarly localized at the xylem parenchyma cells of enlarged vascular bundles of nodes facing toward the xylem vessels. Furthermore, this protein was rapidly degraded within a few hours in response to high B. Knockout of this gene hardly affected the uptake and root-to-shoot translocation of B, but altered B distribution in different organs in the above-ground parts, decreased distribution of B to the new leaves, and increased distribution to the old leaves. These results indicate that OsNIP3;1 located in the nodes is involved in the preferential distribution of B to the developing tissues by unloading B from the xylem in rice and that it is regulated at both transcriptional and protein level in response to external B level.

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The Key to Mn Homeostasis in Plants: Regulation of Mn Transporters

Cited by 157 publications

References 49 publications

Physiological and molecular mechanisms of heavy metal accumulation in nonmycorrhizal versus mycorrhizal plants

Physiological and molecular mechanisms of heavy metal accumulation in nonmycorrhizal versus mycorrhizal plants

Boron demanding tissues of Brassica napus express specific sets of functional Nodulin26‐like Intrinsic Proteins and BOR1 transporters

Preferential Distribution of Boron to Developing Tissues Is Mediated by the Intrinsic Protein OsNIP3

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