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Identification of a ribosome receptor in the rough endoplasmic reticulum

A J Savitz1, D I Meyer

  • 1Department of Biological Chemistry, UCLA School of Medicine 90024.

Nature
|August 9, 1990
PubMed

Insights

Researchers identified a key protein mediating ribosome attachment to the endoplasmic reticulum membrane. This protein

Area of Science:

  • Cell biology
  • Molecular biology
  • Protein transport

Background:

  • Ribosome attachment to the endoplasmic reticulum (ER) membrane is essential for protein secretion in mammalian cells.
  • This process is mediated by specific integral membrane proteins.

Purpose of the Study:

  • To identify and characterize the protein responsible for ribosome-membrane attachment.
  • To investigate the role of the cytosolic domain of this receptor in ribosome binding.

Main Methods:

  • Proteolytic detachment of the cytosolic domain from the ER membrane.
  • Isolation, purification, and characterization of the 180K integral membrane protein.
  • Functional reconstitution of the purified receptor into lipid vesicles.

Main Results:

  • A 180,000 relative molecular mass (Mr 180K) integral membrane protein was identified as the ribosome receptor.
  • The large cytosolic domain (at least 160K) of this protein competitively inhibits ribosome binding.
  • The isolated receptor was successfully reconstituted into lipid vesicles, demonstrating its functionality.

Conclusions:

  • The 180K protein is the primary receptor mediating ribosome attachment to the ER membrane.
  • The cytosolic domain plays a critical role in regulating ribosome binding.
  • The functional reconstitution validates the protein's role in protein transport.

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