Differential Expression of SNAP-25 Protein Isoforms During Divergent Vesicle Fusion Events of Neural Development
The presynaptic plasma membrane protein SNAP-25 (synaptosome-associated protein of 25 kDa) has been implicated as one of several neural-specific components that direct constitutive fusion mechanisms to the regulated vesicle trafficking and exocytosis of neurotransmitter release. There exist two alte...
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| Published in: | Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 5; pp. 1510 - 1514 |
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| Main Authors: | , , , |
| Format: | Journal Article |
| Language: | English |
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United States
National Academy of Sciences of the United States of America
28-02-1995
National Acad Sciences National Academy of Sciences |
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| Abstract | The presynaptic plasma membrane protein SNAP-25 (synaptosome-associated protein of 25 kDa) has been implicated as one of several neural-specific components that direct constitutive fusion mechanisms to the regulated vesicle trafficking and exocytosis of neurotransmitter release. There exist two alternatively spliced isoforms of SNAP-25, a and b, which differ in a putative membrane-interacting domain. We show that these two isoforms have distinct quantitative and anatomical patterns of expression during brain development, in neurons, and in neuroendocrine cells and that the proteins localize differently in neurites of transfected PC12 pheochromocytoma cells. These findings indicate that alternative isoforms of SNAP-25 may play distinct roles in vesicular fusion events required for membrane addition during axonal outgrowth and for release of neuromodulatory peptides and neurotransmitters. |
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| AbstractList | The presynaptic plasma membrane protein SNAP-25 (synaptosome-associated protein of 25 kDa) has been implicated as one of several neural-specific components that direct constitutive fusion mechanisms to the regulated vesicle trafficking and exocytosis of neurotransmitter release. There exist two alternatively spliced isoforms of SNAP-25, a and b, which differ in a putative membrane-interacting domain. We show that these two isoforms have distinct quantitative and anatomical patterns of expression during brain development, in neurons, and in neuroendocrine cells and that the proteins localize differently in neurites of transfected PC12 pheochromocytoma cells. These findings indicate that alternative isoforms of SNAP-25 may play distinct roles in vesicular fusion events required for membrane addition during axonal outgrowth and for release of neuromodulatory peptides and neurotransmitters. The presynaptic plasma membrane protein SNAP-25 (synaptosome-associated protein of 25 kDa) has been implicated as one of several neural-specific components that direct constitutive fusion mechanisms to the regulated vesicle trafficking and exocytosis of neurotransmitter release. Two isoforms of SNAP-25 have distinct quantitative and anatomical patterns of expression during brain development. |
| Author | Bark, I. Christina Ryabinin, Audrey E. Wilson, Michael C. Hahn, Klaus M. |
| AuthorAffiliation | Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA 92037 |
| AuthorAffiliation_xml | – name: Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA 92037 |
| Author_xml | – sequence: 1 givenname: I. Christina surname: Bark fullname: Bark, I. Christina – sequence: 2 givenname: Klaus M. surname: Hahn fullname: Hahn, Klaus M. – sequence: 3 givenname: Audrey E. surname: Ryabinin fullname: Ryabinin, Audrey E. – sequence: 4 givenname: Michael C. surname: Wilson fullname: Wilson, Michael C. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/7878010$$D View this record in MEDLINE/PubMed http://kipublications.ki.se/Default.aspx?queryparsed=id:112813892$$DView record from Swedish Publication Index |
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| Title | Differential Expression of SNAP-25 Protein Isoforms During Divergent Vesicle Fusion Events of Neural Development |
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