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SigmaR1 shapes rough endoplasmic reticulum membrane sheets.

Eric M Sawyer1, Liv E Jensen2, Janet B Meehl1

  • 1Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA; Howard Hughes Medical Institute.

Developmental Cell
|July 6, 2024
PubMed
Summary
This summary is machine-generated.

The sigma-1 receptor (SigmaR1) stabilizes rough endoplasmic reticulum (ER) sheets, crucial for the secretory pathway. SigmaR1 oligomers flatten ER membranes, influencing the quantity of these essential cellular structures.

Keywords:
SigmaR1endoplasmic reticulummembraneorganellepolysometranslation

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Area of Science:

  • Cell Biology
  • Membrane Biology
  • Protein Structure and Function

Background:

  • Rough endoplasmic reticulum (ER) sheets are vital components of the secretory pathway.
  • While reticulons stabilize ER tubules, the proteins scaffolding ER sheets remain largely unknown.

Purpose of the Study:

  • To identify novel protein factors that shape and stabilize rough ER sheets.
  • To elucidate the mechanism by which these factors maintain ER sheet structure.

Main Methods:

  • Proteomics screen using ER sheet-localized RNA-binding proteins.
  • High-resolution live cell imaging and electron tomography.
  • Structure-guided mutagenesis and in vitro reconstitution using giant unilamellar vesicles.

Main Results:

  • The sigma-1 receptor (SigmaR1) was identified as an ER sheet-shaping factor.
  • SigmaR1 levels directly correlate with the abundance of rough ER sheets.
  • SigmaR1 oligomers utilize amphipathic helices to bind and flatten the ER membrane's lumenal leaflet.

Conclusions:

  • SigmaR1 is a key protein that stabilizes rough ER sheets by opposing membrane curvature.
  • SigmaR1's mechanism involves oligomerization and interaction with the ER membrane's lumenal side.
  • This finding expands our understanding of ER membrane organization and the secretory pathway.