Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis in Arabidopsis thaliana

Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus her...

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Published in:Plant direct Vol. 7; no. 5; pp. e495 - n/a
Main Authors: Farthing, Emily C., Henbest, Kate C., Garcia‐Becerra, Tania, Peaston, Kerry A., Williams, Lorraine E.
Format: Journal Article
Language:English
Published: England John Wiley & Sons, Inc 01-05-2023
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Abstract Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans‐Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn‐toxicity tolerance, but only when the cis‐Golgi‐localized MTP11 is non‐functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans‐Golgi‐localized MTP10 plays a role in Mn‐toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non‐functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn‐toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
AbstractList Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans ‐Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn‐toxicity tolerance, but only when the cis ‐Golgi‐localized MTP11 is non‐functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans ‐Golgi‐localized MTP10 plays a role in Mn‐toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non‐functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn‐toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans-Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn-toxicity tolerance, but only when the cis-Golgi-localized MTP11 is non-functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans-Golgi-localized MTP10 plays a role in Mn-toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non-functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn-toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
Abstract Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans‐Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn‐toxicity tolerance, but only when the cis‐Golgi‐localized MTP11 is non‐functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans‐Golgi‐localized MTP10 plays a role in Mn‐toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non‐functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn‐toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans-Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn-toxicity tolerance, but only when the cis-Golgi-localized MTP11 is non-functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans-Golgi-localized MTP10 plays a role in Mn-toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non-functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn-toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the trans-Golgi and plays a major role in response to Mn deficiency with severe effects seen in eca3 nramp1 nramp2 under low Mn supply. ECA3 plays a minor role in Mn-toxicity tolerance, but only when the cis-Golgi-localized MTP11 is non-functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The trans-Golgi-localized MTP10 plays a role in Mn-toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non-functional and when overexpressed in mtp11 mutants. MTP8 and MTP10 confer greater Mn-toxicity resistance to the pmr1 yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of proteins are involved in Mn transport including ECA3, MTPs, and NRAMPs; however, their relative contributions to Mn homeostasis remain to be demonstrated. A major focus here was to clarify the importance of ECA3 in responding to Mn deficiency and toxicity using a range of mutants. We show that ECA3 localizes to the -Golgi and plays a major role in response to Mn deficiency with severe effects seen in under low Mn supply. ECA3 plays a minor role in Mn-toxicity tolerance, but only when the -Golgi-localized MTP11 is non-functional. We also use mutants and overexpressors to determine the relative contributions of MTP members to Mn homeostasis. The -Golgi-localized MTP10 plays a role in Mn-toxicity tolerance, but this is only revealed in mutants when MTP8 and MTP11 are non-functional and when overexpressed in mutants. MTP8 and MTP10 confer greater Mn-toxicity resistance to the yeast mutant than MTP11, and an important role for the first aspartate in the fifth transmembrane domain DxxxD motif is demonstrated. Overall, new insight into the relative influence of key transporters in Mn homeostasis is provided.
Author Garcia‐Becerra, Tania
Henbest, Kate C.
Peaston, Kerry A.
Farthing, Emily C.
Williams, Lorraine E.
AuthorAffiliation 1 School of Biological Sciences University of Southampton Southampton Hampshire UK
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  fullname: Farthing, Emily C.
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  givenname: Kate C.
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  fullname: Henbest, Kate C.
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  givenname: Lorraine E.
  orcidid: 0000-0003-1373-8699
  surname: Williams
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  email: lew@soton.ac.uk
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/37228331$$D View this record in MEDLINE/PubMed
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Copyright 2023 The Authors. published by American Society of Plant Biologists and the Society for Experimental Biology and John Wiley & Sons Ltd.
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Issue 5
Keywords P‐type ATPase
cation diffusion facilitator (CDF)
metal tolerance protein (MTP)
heavy metal
natural resistance‐associated macrophage protein (NRAMP)
transport
manganese
Language English
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This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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  doi: 10.1002/j.1460-2075.1991.tb07696.x
– ident: e_1_2_9_47_1
  doi: 10.1038/sj.emboj.7600864
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Snippet Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn...
Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of proteins are involved in Mn transport...
Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved in Mn...
Abstract Manganese (Mn) is an essential micronutrient for plant growth but becomes toxic when present in excess. A number of Arabidopsis proteins are involved...
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SubjectTerms Agricultural production
cation diffusion facilitator (CDF)
Chloroplasts
Efficiency
Endoplasmic reticulum
Golgi apparatus
heavy metal
Homeostasis
Localization
Manganese
metal tolerance protein (MTP)
Mutants
natural resistance‐associated macrophage protein (NRAMP)
Original Research
Photosynthesis
Proteins
P‐type ATPase
Roles
Toxicity
Toxicity tolerance
transport
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Title Dissecting the relative contribution of ECA3 and group 8/9 cation diffusion facilitators to manganese homeostasis in Arabidopsis thaliana
URI https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fpld3.495
https://www.ncbi.nlm.nih.gov/pubmed/37228331
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