Carl E. Creutz

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Eukaryotic cells contain various Ca(2+)-effector proteins that mediate cellular responses to changes in intracellular Ca(2+) levels. A unique class of these proteins - annexins - can bind to certain membrane phospholipids in a Ca(2+)-dependent manner, providing a link between Ca(2+) signalling and membrane functions. By forming networks on the membrane(More)
The annexins are a group of homologous proteins that bind phospholipids in the presence of calcium. They may provide a major pathway for communication between cellular membranes and their cytoplasmic environment. Annexins have a characteristic "bivalent" activity in the sense that they can draw two membranes together when activated by calcium. This has led(More)
This study investigated mechanisms controlling the nuclear-cytoplasmic partitioning of annexin II (AnxII). AnxII and its ligand, p11, were localized by immunofluorescence to the cytoplasmic compartment of U1242MG cells, with minimal AnxII or p11 detected within nuclei. Similarly, GFP-AnxII and GFP-p11 chimeras localized to the endogenous proteins. Likewise,(More)
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(More)
Several cytosolic proteins bind to secretory granule membranes in a Ca2+-dependent manner and thus may be involved in the mediation of membrane interactions during exocytosis. One of these proteins, calpactin, is a tetramer consisting of two heavy chains of relative molecular mass (Mr) 36K (p36) and two light chains of 10K (p10). We report here that(More)
We provide evidence that copines, members of a ubiquitous family of calcium-dependent, membrane-binding proteins, may represent a universal transduction pathway for calcium signaling because we find copines are capable of interacting with a wide variety of "target" proteins including MEK1, protein phosphatase 5, and the CDC42-regulated kinase, that are(More)
The copines are a novel group of Ca(2+)-dependent, phospholipid-binding proteins first isolated from Paramecium tetraurelia [Creutz, C. E., et al. (1998) J. Biol. Chem. 273, 1393-1402] and found in a wide range of organisms, from plants to humans. They have a Ca(2+) and phospholipid-binding domain consisting of two C2 domains and a core domain in the(More)
We have isolated from the adrenal medulla a protein which causes the aggregation of isolated chromaffin granules when incubated in the presence of free calcium at concentrations greater than 6 PM. The isolation procedure included precipitation in ammonium sulfate, gel filtration, and hydroxylapatite chromatography. Aggregating activity was assayed using(More)
The copines are a novel family of ubiquitous Ca2+-dependent, phospholipid-binding proteins. They contain two Ca2+- and phospholipid-binding domains known as 'C2 domains' present in proteins such as protein kinase C, phospholipase C and synaptotagmin. Copines are thought to be involved in membrane-trafficking phenomena because of their phospholipid-binding(More)