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TitleA structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols.
Journal, issue, pagesScience, Year 2021
Publish dateJan 14, 2021
AuthorsRenhong Yan / Pingping Cao / Wenqi Song / Hongwu Qian / Ximing Du / Hudson W Coates / Xin Zhao / Yaning Li / Shuai Gao / Xin Gong / Ximing Liu / Jianhua Sui / Jianlin Lei / Hongyuan Yang / Andrew J Brown / Qiang Zhou / Chuangye Yan / Nieng Yan /
PubMed AbstractThe SREBP pathway controls cellular homeostasis of sterols. The key players in this pathway, Scap and Insig-1/2, are membrane-embedded sterol sensors. 25-hydroxycholesterol (25HC)-dependent ...The SREBP pathway controls cellular homeostasis of sterols. The key players in this pathway, Scap and Insig-1/2, are membrane-embedded sterol sensors. 25-hydroxycholesterol (25HC)-dependent association of Scap and Insigs acts as the master switch for the SREBP pathway. Here, we present cryo-EM analysis of the human Scap and Insig-2 complex in the presence of 25HC, with the transmembrane (TM) domains determined at an average resolution of 3.7 Å. The sterol sensing domain (SSD) in Scap and all six TMs in Insig-2 were resolved. A 25HC molecule is sandwiched between the S4-S6 segments in Scap and TMs 3/4 in Insig-2 in the luminal leaflet of the membrane. Unwinding of the middle of the Scap-S4 segment is crucial for 25HC binding and Insig association.
External linksScience / PubMed:33446483
MethodsEM (single particle)
Resolution3.7 Å
Structure data

EMDB-30074, PDB-6m49:
cryo-EM structure of Scap/Insig complex in the present of 25-hydroxyl cholesterol.
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-HC3:
25-HYDROXYCHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Scap / Insig / cholesterol / sterol sensing / 25-hydroxycholesterol / SREBP

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