author_facet Skehel, Paul A.
Martin, Kelsey C.
Kandel, Eric R.
Bartsch, Dusan
Skehel, Paul A.
Martin, Kelsey C.
Kandel, Eric R.
Bartsch, Dusan
author Skehel, Paul A.
Martin, Kelsey C.
Kandel, Eric R.
Bartsch, Dusan
spellingShingle Skehel, Paul A.
Martin, Kelsey C.
Kandel, Eric R.
Bartsch, Dusan
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A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
Multidisciplinary
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spelling Skehel, Paul A. Martin, Kelsey C. Kandel, Eric R. Bartsch, Dusan 0036-8075 1095-9203 American Association for the Advancement of Science (AAAS) Multidisciplinary http://dx.doi.org/10.1126/science.7667638 <jats:p> Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP—an integral membrane protein of the vesicle—and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from <jats:italic>Aplysia</jats:italic> that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of <jats:italic>Aplysia</jats:italic> . Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter. </jats:p> A VAMP-Binding Protein from <i>Aplysia</i> Required for Neurotransmitter Release Science
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title A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_unstemmed A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_full A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_fullStr A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_full_unstemmed A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_short A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_sort a vamp-binding protein from <i>aplysia</i> required for neurotransmitter release
topic Multidisciplinary
url http://dx.doi.org/10.1126/science.7667638
publishDate 1995
physical 1580-1583
description <jats:p> Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP—an integral membrane protein of the vesicle—and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from <jats:italic>Aplysia</jats:italic> that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of <jats:italic>Aplysia</jats:italic> . Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter. </jats:p>
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author Skehel, Paul A., Martin, Kelsey C., Kandel, Eric R., Bartsch, Dusan
author_facet Skehel, Paul A., Martin, Kelsey C., Kandel, Eric R., Bartsch, Dusan, Skehel, Paul A., Martin, Kelsey C., Kandel, Eric R., Bartsch, Dusan
author_sort skehel, paul a.
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description <jats:p> Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP—an integral membrane protein of the vesicle—and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from <jats:italic>Aplysia</jats:italic> that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of <jats:italic>Aplysia</jats:italic> . Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter. </jats:p>
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spelling Skehel, Paul A. Martin, Kelsey C. Kandel, Eric R. Bartsch, Dusan 0036-8075 1095-9203 American Association for the Advancement of Science (AAAS) Multidisciplinary http://dx.doi.org/10.1126/science.7667638 <jats:p> Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP—an integral membrane protein of the vesicle—and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from <jats:italic>Aplysia</jats:italic> that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of <jats:italic>Aplysia</jats:italic> . Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter. </jats:p> A VAMP-Binding Protein from <i>Aplysia</i> Required for Neurotransmitter Release Science
spellingShingle Skehel, Paul A., Martin, Kelsey C., Kandel, Eric R., Bartsch, Dusan, Science, A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release, Multidisciplinary
title A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_full A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_fullStr A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_full_unstemmed A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_short A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
title_sort a vamp-binding protein from <i>aplysia</i> required for neurotransmitter release
title_unstemmed A VAMP-Binding Protein from Aplysia Required for Neurotransmitter Release
topic Multidisciplinary
url http://dx.doi.org/10.1126/science.7667638