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Structure of a eukaryotic SWEET transporter in a homotrimeric complex.

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Title: Structure of a eukaryotic SWEET transporter in a homotrimeric complex.
Authors: Tao, Yuyong, Cheung, Lily S., Li, Shuo, Eom, Joon-Seob, Chen, Li-Qing, Xu, Yan, Perry, Kay, Frommer, Wolf B., Feng, Liang
Source: Nature. 11/12/2015, Vol. 527 Issue 7577, p259-263. 5p. 3 Color Photographs, 7 Diagrams, 2 Charts, 2 Graphs.
Subjects: Eukaryotic cells, Plant protein structure, Glucose transporters, Arabidopsis proteins, Rice proteins
Abstract: Eukaryotes rely on efficient distribution of energy and carbon skeletons between organs in the form of sugars. Glucose in animals and sucrose in plants serve as the dominant distribution forms. Cellular sugar uptake and release require vesicular and/or plasma membrane transport proteins. Humans and plants use proteins from three superfamilies for sugar translocation: the major facilitator superfamily (MFS), the sodium solute symporter family (SSF; only in the animal kingdom), and SWEETs. SWEETs carry mono- and disaccharides across vacuolar or plasma membranes. Plant SWEETs play key roles in sugar translocation between compartments, cells, and organs, notably in nectar secretion, phloem loading for long distance translocation, pollen nutrition, and seed filling. Plant SWEETs cause pathogen susceptibility possibly by sugar leakage from infected cells. The vacuolar Arabidopsis thaliana AtSWEET2 sequesters sugars in root vacuoles; loss-of-function mutants show increased susceptibility to Pythium infection. Here we show that its orthologue, the vacuolar glucose transporter OsSWEET2b from rice (Oryza sativa), consists of an asymmetrical pair of triple-helix bundles, connected by an inversion linker transmembrane helix (TM4) to create the translocation pathway. Structural and biochemical analyses show OsSWEET2b in an apparent inward (cytosolic) open state forming homomeric trimers. TM4 tightly interacts with the first triple-helix bundle within a protomer and mediates key contacts among protomers. Structure-guided mutagenesis of the close paralogue SWEET1 from Arabidopsis identified key residues in substrate translocation and protomer crosstalk. Insights into the structure-function relationship of SWEETs are valuable for understanding the transport mechanism of eukaryotic SWEETs and may be useful for engineering sugar flux. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Structure of a eukaryotic SWEET transporter in a homotrimeric complex.
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  Data: <searchLink fieldCode="AR" term="%22Tao%2C+Yuyong%22">Tao, Yuyong</searchLink><br /><searchLink fieldCode="AR" term="%22Cheung%2C+Lily+S%2E%22">Cheung, Lily S.</searchLink><br /><searchLink fieldCode="AR" term="%22Li%2C+Shuo%22">Li, Shuo</searchLink><br /><searchLink fieldCode="AR" term="%22Eom%2C+Joon-Seob%22">Eom, Joon-Seob</searchLink><br /><searchLink fieldCode="AR" term="%22Chen%2C+Li-Qing%22">Chen, Li-Qing</searchLink><br /><searchLink fieldCode="AR" term="%22Xu%2C+Yan%22">Xu, Yan</searchLink><br /><searchLink fieldCode="AR" term="%22Perry%2C+Kay%22">Perry, Kay</searchLink><br /><searchLink fieldCode="AR" term="%22Frommer%2C+Wolf+B%2E%22">Frommer, Wolf B.</searchLink><br /><searchLink fieldCode="AR" term="%22Feng%2C+Liang%22">Feng, Liang</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 11/12/2015, Vol. 527 Issue 7577, p259-263. 5p. 3 Color Photographs, 7 Diagrams, 2 Charts, 2 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Eukaryotic+cells%22">Eukaryotic cells</searchLink><br /><searchLink fieldCode="DE" term="%22Plant+protein+structure%22">Plant protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Glucose+transporters%22">Glucose transporters</searchLink><br /><searchLink fieldCode="DE" term="%22Arabidopsis+proteins%22">Arabidopsis proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Rice+proteins%22">Rice proteins</searchLink>
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  Data: Eukaryotes rely on efficient distribution of energy and carbon skeletons between organs in the form of sugars. Glucose in animals and sucrose in plants serve as the dominant distribution forms. Cellular sugar uptake and release require vesicular and/or plasma membrane transport proteins. Humans and plants use proteins from three superfamilies for sugar translocation: the major facilitator superfamily (MFS), the sodium solute symporter family (SSF; only in the animal kingdom), and SWEETs. SWEETs carry mono- and disaccharides across vacuolar or plasma membranes. Plant SWEETs play key roles in sugar translocation between compartments, cells, and organs, notably in nectar secretion, phloem loading for long distance translocation, pollen nutrition, and seed filling. Plant SWEETs cause pathogen susceptibility possibly by sugar leakage from infected cells. The vacuolar Arabidopsis thaliana AtSWEET2 sequesters sugars in root vacuoles; loss-of-function mutants show increased susceptibility to Pythium infection. Here we show that its orthologue, the vacuolar glucose transporter OsSWEET2b from rice (Oryza sativa), consists of an asymmetrical pair of triple-helix bundles, connected by an inversion linker transmembrane helix (TM4) to create the translocation pathway. Structural and biochemical analyses show OsSWEET2b in an apparent inward (cytosolic) open state forming homomeric trimers. TM4 tightly interacts with the first triple-helix bundle within a protomer and mediates key contacts among protomers. Structure-guided mutagenesis of the close paralogue SWEET1 from Arabidopsis identified key residues in substrate translocation and protomer crosstalk. Insights into the structure-function relationship of SWEETs are valuable for understanding the transport mechanism of eukaryotic SWEETs and may be useful for engineering sugar flux. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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