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Identification of a domain that mediates vesicle aggregation reveals functional diversity of annexin repeats.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1991 Apr 15; Vol. 266 (11), pp. 6670-3. - Publication Year :
- 1991
-
Abstract
- Annexins are structurally related proteins that bind phospholipids in a Ca2(+)-dependent manner and possess at least four conserved 70-amino acid repeat domains. The ability of certain annexins to promote contact between vesicle membranes in vitro has prompted the suggestion that these proteins regulate membrane traffic in exocytosis. We have previously found that annexins I and II promote contact between vesicles whereas annexin V does not. In order to understand the mechanism of annexin I-mediated vesicle-vesicle contact, we prepared a monoclonal antibody that specifically inhibits annexin I-mediated vesicle aggregation. We identified the domain of annexin I recognized by this monoclonal antibody by using it to screen an expression library containing random fragments of annexin I cDNA. The antibody identified a fragment encoding amino acids 41-118 (the first repeat plus 8 residues of the amino-terminal tail). We constructed a chimeric protein containing these amino acids of annexin I fused to the second, third, and fourth repeats of annexin V. Transfer of this domain conferred the ability to promote vesicle aggregation, confirming that this domain participates directly in mediating contact between vesicle membranes.
- Subjects :
- Antibodies, Monoclonal
Base Sequence
Calcium pharmacology
Calcium-Binding Proteins immunology
Calcium-Binding Proteins metabolism
Cell Line
Chimera
Cloning, Molecular
Epitopes analysis
Gene Library
Humans
Liposomes
Molecular Sequence Data
Oligonucleotide Probes
Phosphatidylserines
Polymerase Chain Reaction
Calcium-Binding Proteins genetics
Genetic Variation
Repetitive Sequences, Nucleic Acid
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 266
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1707872