Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Annexins: linking Ca2+ signalling to membrane dynamics
Eukaryotic cells contain various Ca2+-effector proteins that mediate cellular responses to changes in intracellular Ca2+ levels. A unique class of these proteins — annexins — can bind to certain…
The Copines, a Novel Class of C2 Domain-containing, Calciumdependent, Phospholipid-binding Proteins Conserved from Paramecium to Humans*
- C. Creutz, J. L. Tomsig, Jean Cohen
- Biology, ChemistryThe Journal of Biological Chemistry
- 16 January 1998
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 and revealed that copine is a novel protein that contains a C2 domain likely to be responsible for its membrane active properties.
Identification of Targets for Calcium Signaling through the Copine Family of Proteins
Evidence that copines, members of a ubiquitous family of calcium-dependent, membrane-binding proteins, may represent a universal transduction pathway for calcium signaling is provided and a consensus sequence for the coiled-coil copine-binding site was derived and found to have predictive value for identifying new copine targets.
Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
It is reported here that calpactin promotes the Ca2-dependent aggregation and fatty acid-dependent fusion of chromaffin granule membranes at a level of Ca2+ that is lower than that reported for other granule-aggregating proteins, and which parallels theCa2+ requirement for secretion from permeabilized Chromaffin cells.
The annexins and exocytosis.
- C. Creutz
- 6 November 1992
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…
Control of the nuclear-cytoplasmic partitioning of annexin II by a nuclear export signal and by p11 binding.
Investigation of mechanisms controlling the nuclear-cytoplasmic partitioning of annexin II found that AnxII monomer can enter the nucleus and is actively exported, however, LmB had little effect on the localization of Anxii/p11 complex in U1242MG cells, indicating that the complex is sequestered in the cy toplasm.
Characterization of the yeast tricalbins: membrane-bound multi-C2-domain proteins that form complexes involved in membrane trafficking
The results suggest that the tricalbins function as multimers in membrane-trafficking events and may provide insights into the roles of multi-C2-domain proteins, such as the synaptotagmins, in other organisms.
Internal pH and state of ATP in adrenergic chromaffin granules determined by 31P nuclear magnetic resonance spectroscopy.
- H. Pollard, H. Shindo, C. Creutz, C. Pazoles, J. Cohen
- BiologyThe Journal of biological chemistry
- 25 February 1979
This work reversibly adjusted the internal pH of granules to different values by adding weak acid (acetate), weak base (ammonia), or nigericin/K+, which equalize the internal and external pH values, and found that the intragranular pH was 5.7, a value consistent with independent methods.
Copines: a ubiquitous family of Ca2+-dependent phospholipid-binding proteins
The biochemistry, gene structure, tissue distribution and possible biological roles of copines are discussed, including recent observations with Arabidopsis that indicate that copines may be involved in cell division and growth.