Cryo-EM structure supports a role of AQP7 as a junction protein

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Standard

Cryo-EM structure supports a role of AQP7 as a junction protein. / Huang, Peng; Venskutonytė, Raminta; Prasad, Rashmi B; Ardalani, Hamidreza; de Maré, Sofia W; Fan, Xiao; Li, Ping; Spégel, Peter; Yan, Nieng; Gourdon, Pontus; Artner, Isabella; Lindkvist-Petersson, Karin.

I: Nature Communications, Bind 14, Nr. 1, 600, 2023.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Huang, P, Venskutonytė, R, Prasad, RB, Ardalani, H, de Maré, SW, Fan, X, Li, P, Spégel, P, Yan, N, Gourdon, P, Artner, I & Lindkvist-Petersson, K 2023, 'Cryo-EM structure supports a role of AQP7 as a junction protein', Nature Communications, bind 14, nr. 1, 600. https://doi.org/10.1038/s41467-023-36272-y

APA

Huang, P., Venskutonytė, R., Prasad, R. B., Ardalani, H., de Maré, S. W., Fan, X., Li, P., Spégel, P., Yan, N., Gourdon, P., Artner, I., & Lindkvist-Petersson, K. (2023). Cryo-EM structure supports a role of AQP7 as a junction protein. Nature Communications, 14(1), [600]. https://doi.org/10.1038/s41467-023-36272-y

Vancouver

Huang P, Venskutonytė R, Prasad RB, Ardalani H, de Maré SW, Fan X o.a. Cryo-EM structure supports a role of AQP7 as a junction protein. Nature Communications. 2023;14(1). 600. https://doi.org/10.1038/s41467-023-36272-y

Author

Huang, Peng ; Venskutonytė, Raminta ; Prasad, Rashmi B ; Ardalani, Hamidreza ; de Maré, Sofia W ; Fan, Xiao ; Li, Ping ; Spégel, Peter ; Yan, Nieng ; Gourdon, Pontus ; Artner, Isabella ; Lindkvist-Petersson, Karin. / Cryo-EM structure supports a role of AQP7 as a junction protein. I: Nature Communications. 2023 ; Bind 14, Nr. 1.

Bibtex

@article{8a3e3d847c044fd69e4cdee1c55a6cc7,

title = "Cryo-EM structure supports a role of AQP7 as a junction protein",

abstract = "Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 {\AA} resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.",

keywords = "Humans, Aquaglyceroporins, Aquaporins/metabolism, Glycerol/metabolism, Cryoelectron Microscopy, Islets of Langerhans/metabolism",

author = "Peng Huang and Raminta Venskutonytė and Prasad, {Rashmi B} and Hamidreza Ardalani and {de Mar{\'e}}, {Sofia W} and Xiao Fan and Ping Li and Peter Sp{\'e}gel and Nieng Yan and Pontus Gourdon and Isabella Artner and Karin Lindkvist-Petersson",

note = "{\textcopyright} 2023. The Author(s).",

year = "2023",

doi = "10.1038/s41467-023-36272-y",

language = "English",

volume = "14",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "nature publishing group",

number = "1",

}

RIS

TY - JOUR

T1 - Cryo-EM structure supports a role of AQP7 as a junction protein

AU - Huang, Peng

AU - Venskutonytė, Raminta

AU - Prasad, Rashmi B

AU - Ardalani, Hamidreza

AU - de Maré, Sofia W

AU - Fan, Xiao

AU - Li, Ping

AU - Spégel, Peter

AU - Yan, Nieng

AU - Gourdon, Pontus

AU - Artner, Isabella

AU - Lindkvist-Petersson, Karin

PY - 2023

Y1 - 2023

N2 - Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.

AB - Aquaglyceroporin 7 (AQP7) facilitates glycerol flux across the plasma membrane with a critical physiological role linked to metabolism, obesity, and associated diseases. Here, we present the single-particle cryo-EM structure of AQP7 determined at 2.55 Å resolution adopting two adhering tetramers, stabilized by extracellularly exposed loops, in a configuration like that of the well-characterized interaction of AQP0 tetramers. The central pore, in-between the four monomers, displays well-defined densities restricted by two leucine filters. Gas chromatography mass spectrometry (GC/MS) results show that the AQP7 sample contains glycerol 3-phosphate (Gro3P), which is compatible with the identified features in the central pore. AQP7 is shown to be highly expressed in human pancreatic α- and β- cells suggesting that the identified AQP7 octamer assembly, in addition to its function as glycerol channel, may serve as junction proteins within the endocrine pancreas.

KW - Humans

KW - Aquaglyceroporins

KW - Aquaporins/metabolism

KW - Glycerol/metabolism

KW - Cryoelectron Microscopy

KW - Islets of Langerhans/metabolism

U2 - 10.1038/s41467-023-36272-y

DO - 10.1038/s41467-023-36272-y

M3 - Journal article

C2 - 36737436

VL - 14

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 600

ER -

ID: 338428304