Bilayer STING goes head to head to stay put

Kun Yang; Nan Yan

doi:10.1016/j.molcel.2023.04.004

Bilayer STING goes head to head to stay put

Kun Yang, Nan Yan

Research output: Contribution to journal › Comment/debate › peer-review

1 Scopus citations

Abstract

In this issue, Liu et al.¹ provide structural insights into how STING remains inactive. Apo-STING adopts a bilayer conformation exhibiting head-to-head and side-to-side interactions in its autoinhibitory state on the ER. The apo-STING oligomer differs from the activated STING oligomer in its biochemical stability, protein domain contact, and membrane curvature.

Original language	English (US)
Pages (from-to)	1372-1374
Number of pages	3
Journal	Molecular cell
Volume	83
Issue number	9
DOIs	https://doi.org/10.1016/j.molcel.2023.04.004
State	Published - May 4 2023

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2023.04.004

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title = "Bilayer STING goes head to head to stay put",

abstract = "In this issue, Liu et al.1 provide structural insights into how STING remains inactive. Apo-STING adopts a bilayer conformation exhibiting head-to-head and side-to-side interactions in its autoinhibitory state on the ER. The apo-STING oligomer differs from the activated STING oligomer in its biochemical stability, protein domain contact, and membrane curvature.",

author = "Kun Yang and Nan Yan",

note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Inc.",

year = "2023",

month = may,

day = "4",

doi = "10.1016/j.molcel.2023.04.004",

language = "English (US)",

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pages = "1372--1374",

journal = "Molecular cell",

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number = "9",

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T1 - Bilayer STING goes head to head to stay put

AU - Yang, Kun

AU - Yan, Nan

PY - 2023/5/4

Y1 - 2023/5/4

N2 - In this issue, Liu et al.1 provide structural insights into how STING remains inactive. Apo-STING adopts a bilayer conformation exhibiting head-to-head and side-to-side interactions in its autoinhibitory state on the ER. The apo-STING oligomer differs from the activated STING oligomer in its biochemical stability, protein domain contact, and membrane curvature.

AB - In this issue, Liu et al.1 provide structural insights into how STING remains inactive. Apo-STING adopts a bilayer conformation exhibiting head-to-head and side-to-side interactions in its autoinhibitory state on the ER. The apo-STING oligomer differs from the activated STING oligomer in its biochemical stability, protein domain contact, and membrane curvature.

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U2 - 10.1016/j.molcel.2023.04.004

DO - 10.1016/j.molcel.2023.04.004

M3 - Comment/debate

C2 - 37146568

AN - SCOPUS:85153518498

SN - 1097-2765

VL - 83

SP - 1372

EP - 1374

JO - Molecular cell

JF - Molecular cell

IS - 9

ER -

Bilayer STING goes head to head to stay put

Abstract

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