Golgi localized barley MTP8 proteins facilitate Mn transport

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Golgi localized barley MTP8 proteins facilitate Mn transport. / Pedas, Pai Rosager; Schiller, Michaela; Hegelund, Josefine Nymark; Ladegaard, Anne Hald; Schjørring, Jan Kofod; Husted, Søren.

In: PLOS ONE, Vol. 9, No. 12, e113759, 2014.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Pedas, PR, Schiller, M, Hegelund, JN, Ladegaard, AH, Schjørring, JK & Husted, S 2014, 'Golgi localized barley MTP8 proteins facilitate Mn transport', PLOS ONE, vol. 9, no. 12, e113759. https://doi.org/10.1371/journal.pone.0113759

APA

Pedas, P. R., Schiller, M., Hegelund, J. N., Ladegaard, A. H., Schjørring, J. K., & Husted, S. (2014). Golgi localized barley MTP8 proteins facilitate Mn transport. PLOS ONE, 9(12), [e113759]. https://doi.org/10.1371/journal.pone.0113759

Vancouver

Pedas PR, Schiller M, Hegelund JN, Ladegaard AH, Schjørring JK, Husted S. Golgi localized barley MTP8 proteins facilitate Mn transport. PLOS ONE. 2014;9(12). e113759. https://doi.org/10.1371/journal.pone.0113759

Author

Pedas, Pai Rosager ; Schiller, Michaela ; Hegelund, Josefine Nymark ; Ladegaard, Anne Hald ; Schjørring, Jan Kofod ; Husted, Søren. / Golgi localized barley MTP8 proteins facilitate Mn transport. In: PLOS ONE. 2014 ; Vol. 9, No. 12.

Bibtex

@article{73b40579086c432bb8f7818157ec1f49,
title = "Golgi localized barley MTP8 proteins facilitate Mn transport",
abstract = "Many metabolic processes in plants are regulated by manganese (Mn) but limited information is available on the molecular mechanisms controlling cellular Mn homeostasis. In this study, a yeast assay was used to isolate and characterize two genes, MTP8.1 and MTP8.2 , which encode membrane-bound proteins belonging to the cation diffusion facilitator (CDF) family in the cereal species barley (Hordeum vulgare). Transient expression in onion epidermal cells showed that MTP8.1 and MTP8.2 proteins fused to the green fluorescent protein (GFP) are localized to Golgi. When heterologously expressed in yeast, MTP8.1 and MTP8.2 were found to be Mn transporters catalysing Mn efflux in a similar manner as the Golgi localized endogenous yeast protein Pmr1p. The level of MTP8.1 transcripts in barley roots increased with external Mn supply ranging from deficiency to toxicity, while MTP8.2 transcripts decreased under the same conditions, indicating non-overlapping functions for the two genes. In barley leaves, the expression of both MTP8 genes declined in response to toxic Mn additions to the roots suggesting a role in ensuring proper delivery of Mn to Golgi. Based on the above we suggest that barley MTP8 proteins are involved in Mn loading to the Golgi apparatus and play a role in Mn homeostasis by delivering Mn to Mn-dependent enzymes and/or by facilitating Mn efflux via secretory vesicles. This study highlights the importance of MTP transporters in Mn homeostasis and is the first report of Golgi localized Mn2+transport proteins in a monocot plant species.",
author = "Pedas, {Pai Rosager} and Michaela Schiller and Hegelund, {Josefine Nymark} and Ladegaard, {Anne Hald} and Schj{\o}rring, {Jan Kofod} and S{\o}ren Husted",
note = "OA",
year = "2014",
doi = "10.1371/journal.pone.0113759",
language = "English",
volume = "9",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "12",

}

RIS

TY - JOUR

T1 - Golgi localized barley MTP8 proteins facilitate Mn transport

AU - Pedas, Pai Rosager

AU - Schiller, Michaela

AU - Hegelund, Josefine Nymark

AU - Ladegaard, Anne Hald

AU - Schjørring, Jan Kofod

AU - Husted, Søren

N1 - OA

PY - 2014

Y1 - 2014

N2 - Many metabolic processes in plants are regulated by manganese (Mn) but limited information is available on the molecular mechanisms controlling cellular Mn homeostasis. In this study, a yeast assay was used to isolate and characterize two genes, MTP8.1 and MTP8.2 , which encode membrane-bound proteins belonging to the cation diffusion facilitator (CDF) family in the cereal species barley (Hordeum vulgare). Transient expression in onion epidermal cells showed that MTP8.1 and MTP8.2 proteins fused to the green fluorescent protein (GFP) are localized to Golgi. When heterologously expressed in yeast, MTP8.1 and MTP8.2 were found to be Mn transporters catalysing Mn efflux in a similar manner as the Golgi localized endogenous yeast protein Pmr1p. The level of MTP8.1 transcripts in barley roots increased with external Mn supply ranging from deficiency to toxicity, while MTP8.2 transcripts decreased under the same conditions, indicating non-overlapping functions for the two genes. In barley leaves, the expression of both MTP8 genes declined in response to toxic Mn additions to the roots suggesting a role in ensuring proper delivery of Mn to Golgi. Based on the above we suggest that barley MTP8 proteins are involved in Mn loading to the Golgi apparatus and play a role in Mn homeostasis by delivering Mn to Mn-dependent enzymes and/or by facilitating Mn efflux via secretory vesicles. This study highlights the importance of MTP transporters in Mn homeostasis and is the first report of Golgi localized Mn2+transport proteins in a monocot plant species.

AB - Many metabolic processes in plants are regulated by manganese (Mn) but limited information is available on the molecular mechanisms controlling cellular Mn homeostasis. In this study, a yeast assay was used to isolate and characterize two genes, MTP8.1 and MTP8.2 , which encode membrane-bound proteins belonging to the cation diffusion facilitator (CDF) family in the cereal species barley (Hordeum vulgare). Transient expression in onion epidermal cells showed that MTP8.1 and MTP8.2 proteins fused to the green fluorescent protein (GFP) are localized to Golgi. When heterologously expressed in yeast, MTP8.1 and MTP8.2 were found to be Mn transporters catalysing Mn efflux in a similar manner as the Golgi localized endogenous yeast protein Pmr1p. The level of MTP8.1 transcripts in barley roots increased with external Mn supply ranging from deficiency to toxicity, while MTP8.2 transcripts decreased under the same conditions, indicating non-overlapping functions for the two genes. In barley leaves, the expression of both MTP8 genes declined in response to toxic Mn additions to the roots suggesting a role in ensuring proper delivery of Mn to Golgi. Based on the above we suggest that barley MTP8 proteins are involved in Mn loading to the Golgi apparatus and play a role in Mn homeostasis by delivering Mn to Mn-dependent enzymes and/or by facilitating Mn efflux via secretory vesicles. This study highlights the importance of MTP transporters in Mn homeostasis and is the first report of Golgi localized Mn2+transport proteins in a monocot plant species.

U2 - 10.1371/journal.pone.0113759

DO - 10.1371/journal.pone.0113759

M3 - Journal article

C2 - 25486417

AN - SCOPUS:84915747216

VL - 9

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 12

M1 - e113759

ER -

ID: 130100843