Calcium‐Dependent Dissociation of Synaptotagmin from Synaptic SNARE Complexes
: The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca2+‐dependent regulation of exocytosis. However, the subcellular compartm...
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Published in | Journal of neurochemistry Vol. 74; no. 1; pp. 367 - 374 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Oxford UK
Blackwell Science Ltd
01.01.2000
Blackwell |
Subjects | |
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Abstract | : The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca2+‐dependent regulation of exocytosis. However, the subcellular compartments in which interactions occur and their modulation by Ca2+ influx remain obscure. Sodium dodecyl sulfate (SDS)‐resistant core complexes, associated with synaptotagmin I, were enriched in rat brain fractions containing plasma membranes and docked synaptic vesicles. Depolarization of synaptosomes triggered [3H]GABA release and Ca2+‐dependent dissociation of synaptotagmin from the core complex. In perforated synaptosomes, synaptotagmin dissociation was induced by Ca2+ (30‐300 μM) but not Sr2+ (1 mM); it apparently required intact membrane bilayers but did not result in disassembly of trimeric SNARE complexes. Synaptotagmin was not associated with unstable v‐SNARE/t‐SNARE complexes, present in fractions containing synaptic vesicles and cytoplasm. These complexes acquired SDS resistance when N‐ethylmaleimide‐sensitive fusion protein (NSF) was inhibited with N‐ethylmaleimide or adenosine 5′‐O‐(3‐thiotriphosphate), suggesting that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Our findings are consistent with models in which the Ca2+‐triggered release of synaptotagmin precedes vesicle fusion. NSF may then dissociate ternary core complexes captured by endocytosis and recycle/prime individual SNARE proteins. |
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AbstractList | The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca2+-dependent regulation of exocytosis. However, the subcellular compartments in which interactions occur and their modulation by Ca2+ influx remain obscure. Sodium dodecyl sulfate (SDS)-resistant core complexes, associated with synaptotagmin I, were enriched in rat brain fractions containing plasma membranes and docked synaptic vesicles. Depolarization of synaptosomes triggered [3H]GABA release and Ca2+-dependent dissociation of synaptotagmin from the core complex. In perforated synaptosomes, synaptotagmin dissociation was induced by Ca2+ (30-300 microM) but not Sr2+ (1 mM); it apparently required intact membrane bilayers but did not result in disassembly of trimeric SNARE complexes. Synaptotagmin was not associated with unstable v-SNARE/t-SNARE complexes, present in fractions containing synaptic vesicles and cytoplasm. These complexes acquired SDS resistance when N-ethylmaleimide-sensitive fusion protein (NSF) was inhibited with N-ethylmaleimide or adenosine 5'-O-(3-thiotriphosphate), suggesting that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Our findings are consistent with models in which the Ca2+ triggered release of synaptotagmin precedes vesicle fusion. NSF may then dissociate ternary core complexes captured by endocytosis and recycle/prime individual SNARE proteins. : The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca2+‐dependent regulation of exocytosis. However, the subcellular compartments in which interactions occur and their modulation by Ca2+ influx remain obscure. Sodium dodecyl sulfate (SDS)‐resistant core complexes, associated with synaptotagmin I, were enriched in rat brain fractions containing plasma membranes and docked synaptic vesicles. Depolarization of synaptosomes triggered [3H]GABA release and Ca2+‐dependent dissociation of synaptotagmin from the core complex. In perforated synaptosomes, synaptotagmin dissociation was induced by Ca2+ (30‐300 μM) but not Sr2+ (1 mM); it apparently required intact membrane bilayers but did not result in disassembly of trimeric SNARE complexes. Synaptotagmin was not associated with unstable v‐SNARE/t‐SNARE complexes, present in fractions containing synaptic vesicles and cytoplasm. These complexes acquired SDS resistance when N‐ethylmaleimide‐sensitive fusion protein (NSF) was inhibited with N‐ethylmaleimide or adenosine 5′‐O‐(3‐thiotriphosphate), suggesting that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Our findings are consistent with models in which the Ca2+‐triggered release of synaptotagmin precedes vesicle fusion. NSF may then dissociate ternary core complexes captured by endocytosis and recycle/prime individual SNARE proteins. The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca 2+ ‐dependent regulation of exocytosis. However, the subcellular compartments in which interactions occur and their modulation by Ca 2+ influx remain obscure. Sodium dodecyl sulfate (SDS)‐resistant core complexes, associated with synaptotagmin I, were enriched in rat brain fractions containing plasma membranes and docked synaptic vesicles. Depolarization of synaptosomes triggered [ 3 H]GABA release and Ca 2+ ‐dependent dissociation of synaptotagmin from the core complex. In perforated synaptosomes, synaptotagmin dissociation was induced by Ca 2+ (30‐300 μ M ) but not Sr 2+ (1 m M ); it apparently required intact membrane bilayers but did not result in disassembly of trimeric SNARE complexes. Synaptotagmin was not associated with unstable v‐SNARE/t‐SNARE complexes, present in fractions containing synaptic vesicles and cytoplasm. These complexes acquired SDS resistance when N ‐ethylmaleimide‐sensitive fusion protein (NSF) was inhibited with N ‐ethylmaleimide or adenosine 5′‐ O ‐(3‐thiotriphosphate), suggesting that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Our findings are consistent with models in which the Ca 2+ ‐triggered release of synaptotagmin precedes vesicle fusion. NSF may then dissociate ternary core complexes captured by endocytosis and recycle/prime individual SNARE proteins. The formation of the synaptic core (SNARE) complex constitutes a crucial step in synaptic vesicle fusion at the nerve terminal. The interaction of synaptotagmin I with this complex potentially provides a means of conferring Ca super(2+)-dependent regulation of exocytosis. However, the subcellular compartments in which interactions occur and their modulation by Ca super(2+) influx remain obscure. Sodium dodecyl sulfate (SDS)-resistant core complexes, associated with synaptotagmin I, were enriched in rat brain fractions containing plasma membranes and docked synaptic vesicles. Depolarization of synaptosomes triggered [ super(3)H]GABA release and Ca super(2+)-dependent dissociation of synaptotagmin from the core complex. In perforated synaptosomes, synaptotagmin dissociation was induced by Ca super(2+) (30-300 mu M) but not Sr super(2+) (1 mM); it apparently required intact membrane bilayers but did not result in disassembly of trimeric SNARE complexes. Synaptotagmin was not associated with unstable v-SNARE/t-SNARE complexes, present in fractions containing synaptic vesicles and cytoplasm. These complexes acquired SDS resistance when N-ethylmaleimide-sensitive fusion protein (NSF) was inhibited with N-ethylmaleimide or adenosine 5'-O-(3-thiotriphosphate), suggesting that constitutive SNARE complex disassembly occurs in undocked synaptic vesicles. Our findings are consistent with models in which the Ca super(2+)-triggered release of synaptotagmin precedes vesicle fusion. NSF may then dissociate ternary core complexes captured by endocytosis and recycle/prime individual SNARE proteins. |
Author | Leveque, Christian Boudier, Jeanne‐Andree Takahashi, Masami Seagar, Michael |
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Keywords | Vertebrata Synaptosome Mammalia Calcium Rat Synaptic transmission Rodentia Synaptic vesicle Molecular complex Synaptotagmin Exocytosis In vitro |
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Notes | ATPγS, adenosine 5 (3‐thiotriphosphate); BSA, bovine serum albumin; MBP‐syt I, synaptotagmin I fused to maltose binding protein; NEM ethylmaleimide; NSF, NEM‐sensitive fusion protein; PAGE, polyacrylamide gel electrophoresis; SDS, sodium dodecyl sulfate; SNAP, soluble NSF attachment protein; SNAP‐25, synaptosomal‐associated protein of 25 kDa; SNARE, soluble NSF attachment protein receptor; VAMP, vesicle‐associated membrane protein. N Abbreviations used O ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
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SubjectTerms | Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - pharmacology Animals Biological and medical sciences Brain - drug effects Brain - metabolism Calcium - physiology Calcium-Binding Proteins Carrier Proteins - antagonists & inhibitors Cell Membrane - metabolism Cell physiology Drug Resistance Endocytosis Ethylmaleimide - pharmacology Exocytosis Exocytosis - physiology Fundamental and applied biological sciences. Psychology Membrane Glycoproteins - metabolism Membrane Proteins - metabolism Molecular and cellular biology N-Ethylmaleimide-Sensitive Proteins Nerve Tissue Proteins - metabolism N‐Ethylmaleimide‐sensitive fusion protein Rats SNARE complex SNARE Proteins Sodium Dodecyl Sulfate - pharmacology Synapses - metabolism Synaptic vesicle Synaptic Vesicles - metabolism Synaptosomal‐associated protein of 25 kDa Synaptotagmin I Synaptotagmins Syntaxin Vesicle‐associated membrane protein Vesicular Transport Proteins |
Title | Calcium‐Dependent Dissociation of Synaptotagmin from Synaptic SNARE Complexes |
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