An internal signal sequence: the asialoglycoprotein receptor membrane anchor
Cell
|January 17, 1986
Summary
The human asialoglycoprotein receptor H1
Area of Science:
- Molecular biology
- Cell biology
- Biochemistry
Background:
- The human asialoglycoprotein receptor H1 (ASGPR1) is a type I membrane protein.
- Its structure includes a cytoplasmic N-terminus, a transmembrane domain, and an exoplasmic C-terminus.
Purpose of the Study:
- To investigate the mechanism of membrane insertion and glycosylation of ASGPR1.
- To determine the role of the transmembrane domain in these processes.
Main Methods:
- Site-directed mutagenesis to delete the transmembrane domain.
- In vitro translation and translocation assays.
- Signal recognition particle (SRP) dependency assays.
- Glycosylation analysis.
Main Results:
- ASGPR1 membrane insertion and glycosylation are cotranslational and SRP-dependent.
- The transmembrane domain is essential for both membrane insertion and glycosylation.
- The transmembrane domain alone is sufficient to initiate translocation of a heterologous protein.
Conclusions:
- ASGPR1 utilizes a helical hairpin mechanism for membrane insertion.
- This mechanism applies to both cleaved N-terminal and uncleaved internal signal sequences.
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