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Vol. 273, Issue 3, 1393-1402, January 16, 1998
From the In an attempt to identify proteins that might
underlie membrane trafficking processes in ciliates,
calcium-dependent, phospholipid-binding proteins were
isolated from extracts of Paramecium tetraurelia. The major
protein obtained, named copine, had a mass of 55 kDa, bound
phosphatidylserine but not phosphatidylcholine at micromolar levels of
calcium but not magnesium, and promoted lipid vesicle aggregation. The
sequence of a 920-base pair partial cDNA revealed that copine is a
novel protein that contains a C2 domain likely to be responsible for
its membrane active properties. Paramecium was found to
have two closely related copine genes, CPN1 and
CPN2. Current sequence data bases indicate the presence of
multiple copine homologs in green plants, nematodes, and humans. The
full-length sequences reveal that copines consist of two C2 domains at
the N terminus followed by a domain similar to the A domain that
mediates interactions between integrins and extracellular ligands. A
human homolog, copine I, was expressed in bacteria as a fusion protein with glutathione S-transferase. This recombinant protein
exhibited calcium-dependent phospholipid binding
properties similar to those of Paramecium copine. An
antiserum raised against a fragment of human copine I was used to
identify chromobindin 17, a secretory vesicle-binding protein, as a
copine. This association with secretory vesicles, as well the general
ability of copines to bind phospholipid bilayers in a
calcium-dependent manner, suggests that these proteins may
function in membrane trafficking.
The Copines, a Novel Class of C2 Domain-containing,
Calciumdependent, Phospholipid-binding Proteins Conserved
from Paramecium to Humans
§,,,§, Department of Pharmacology, University of
Virginia, Charlottesville, Virginia 22908 and § Centre
de Genetique Moleculaire, Centre National de la Recherche Scientifique,
91198 Gif-sur-Yvette, France
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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