NDLI: Structure of a eukaryotic SWEET transporter in a homo-trimericcomplex

Content Provider	PubMed Central
Author	Tao, Yuyong Cheung, Lily S. Shuo, Li Eom, Joon-seob Chen, Li-qing Yan, Xu Perry, Kay Frommer, Wolf B. Feng, Liang
Abstract	Eukaryotes rely on efficient distribution of energy and carbon skeletonsbetween organs in the form of sugars. Glucose in animals and sucrose in plantsserve as dominant distribution forms. Cellular sugar uptake and release requirevesicular and/or plasma membrane transport proteins. Humans and plants userelated proteins from three superfamilies for sugar translocation: the majorfacilitator superfamily (MFS), the sodium solute symporter Family (SSF; onlyanimal kingdom), and SWEETs 1-5 . SWEETs carry mono- anddisaccharides 6 acrossvacuolar or plasma membranes. Plant SWEETs play key roles in sugar translocationbetween compartments, cells, and organs, notably in nectar secretion 7 , phloem loading for longdistance translocation 8 , pollennutrition 9 , and seedfilling 10 . PlantSWEETs cause pathogen susceptibility by sugar leakage from infectedcells 3,11,12 . Thevacuolar AtSWEET2 sequesters sugars in root vacuoles; loss-of-function increasessusceptibility to Pythium infection 13 . Here we show that its orthologue, thevacuolar glucose transporter OsSWEET2b from rice, consists of an asymmetricalpair of triple-helix-bundles (THBs), connected by an inversion linker helix(TM4) to create the translocation pathway. Structural and biochemical analysesshow OsSWEET2b in an apparent inward (cytosolic) open state forming homomerictrimers. TM4 tightly interacts with the first THB within a protomer and mediateskey contacts among protomers. Structure-guided mutagenesis of the closeparalogue SWEET1 from Arabidopsis identified key residues insubstrate translocation and protomer crosstalk. Insights into thestructure-function relationship of SWEETs is valuable for understanding thetransport mechanism of eukaryotic SWEETs and may be useful for engineering sugarflux.
Related Links	http://dx.doi.org/10.1038/nature15391
Ending Page	263
Page Count	5
Starting Page	259
File Format	PDF
ISSN	14764687
e-ISSN	14764687
Journal	Nature
Issue Number	7577
Volume Number	527
Language	English
Publisher Date	2015-11-12
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
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