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PMID: 2466848 Published · ppublish English Journal Article

Analysis of the signal for attachment of a glycophospholipid membrane anchor.

The Journal of cell biology ·Vol. 108 ·No. 4 ·1989-04-00 ·Pages 1387-96

Caras IW, Weddell GN, Williams SR

Abstract

The COOH terminus of decay accelerating factor (DAF) contains a signal that directs attachment of a glycophospholipid (GPI) membrane anchor. To define this signal we deleted portions of the DAF COOH terminus and expressed the mutant cDNAs it CV1 origin-deficient SV-40 cells. Our results show that the COOH-terminal hydrophobic domain (17 residues) is absolutely required for GPI anchor attachment. However, when fused to the COOH terminus of a secreted protein this hydrophobic domain is insufficient to direct attachment of a GPI anchor. Additional specific information located within the adjacent 20 residues appears to be necessary. We speculate that by analogy with signal sequences for membrane translocation, GPI anchor attachment requires both a COOH-terminal hydrophobic domain (the GPI signal) as well as a suitable cleavage/attachment site located NH2 terminal to the signal.

MeSH Terms
Amino Acid Sequence Animals CD55 Antigens Cell Line Cell Membrane/metabolism Fluorescent Antibody Technique Glycolipids/metabolism Membrane Lipids/metabolism Membrane Proteins/genetics,metabolism Molecular Sequence Data Mutation Phospholipids/metabolism Protein Sorting Signals/genetics Simian virus 40/genetics Transfection
Chemicals
CD55 Antigens Glycolipids Membrane Lipids Membrane Proteins Phospholipids Protein Sorting Signals
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Caras I W
Genentech, Inc., South San Francisco, California 94080.
Weddell G N
Williams S R
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33 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.108.4.1387
Published
1989-04-00
Pages
1387-96
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2115511
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.108.4.1387 PMC Full Text View journal details
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