Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis. 1995

C B Gundersen, and A Mastrogiacomo, and J A Umbach
Department of Molecular and Medical Pharmacology, UCLA School of Medicine 90095, USA.

Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. We propose two distinct pathways to explain how these capabilities might subserve membrane fusion and exocytosis.

UI MeSH Term Description Entries
D008561 Membrane Fusion The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes. Fusion, Membrane,Fusions, Membrane,Membrane Fusions
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D009419 Nerve Tissue Proteins Proteins, Nerve Tissue,Tissue Proteins, Nerve
D005089 Exocytosis Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013572 Synaptic Vesicles Membrane-bound compartments which contain transmitter molecules. Synaptic vesicles are concentrated at presynaptic terminals. They actively sequester transmitter molecules from the cytoplasm. In at least some synapses, transmitter release occurs by fusion of these vesicles with the presynaptic membrane, followed by exocytosis of their contents. Synaptic Vesicle,Vesicle, Synaptic,Vesicles, Synaptic
D050956 HSP40 Heat-Shock Proteins A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins. DnaJ Protein,HSP40 Heat-Shock Protein,HSP40 Protein,Heat-Shock Proteins 40,DnaJ Proteins,HSP40 Protein Family,HSP40 Proteins,Heat Shock Protein 40 Family,Heat-Shock Protein 40,HSP40 Heat Shock Protein,HSP40 Heat Shock Proteins,Heat Shock Protein 40,Heat Shock Proteins 40,Heat-Shock Protein, HSP40,Heat-Shock Proteins, HSP40,Protein, DnaJ,Protein, HSP40,Protein, HSP40 Heat-Shock,Proteins, HSP40 Heat-Shock

Related Publications

C B Gundersen, and A Mastrogiacomo, and J A Umbach
January 1994, Advances in second messenger and phosphoprotein research,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
March 1994, Cell,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
January 1995, Progress in brain research,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
January 1993, Journal of cell science. Supplement,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
June 2002, The Biochemical journal,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
October 1998, The Biochemical journal,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
December 2011, Cold Spring Harbor perspectives in biology,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
October 1981, JAMA,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
December 1997, The Journal of biological chemistry,
C B Gundersen, and A Mastrogiacomo, and J A Umbach
August 1994, Progress in neurobiology,
Copied contents to your clipboard!