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
Main Authors: Bark, I. Christina, Hahn, Klaus M., Ryabinin, Audrey E., Wilson, Michael C.
Format: Journal Article
Language:English
Published: 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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Summary: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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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.92.5.1510