Analysis of the structure and expression of the VAMP family of synaptic vesicle proteins.

VAMP/synaptobrevin proteins were first discovered as small integral membrane proteins in synaptic vesicles of vertebrates and invertebrates. At least two isoforms are expressed in the central nervous system of mammals in non-overlapping patterns. Biochemical studies have revealed that the VAMP synaptic vesicle proteins are the specific target in the presynaptic nerve terminal of botulinum B neurotoxin and tetanus toxin metalloendoprotease activities. The fact that these toxins rapidly and completely abrogate neurotransmission suggests that VAMP proteins play an essential role in this process. More recently, immunologically related proteins have been identified in non-neuronal cells such as adipocytes. In addition, molecular genetic studies of yeast secretion have identified VAMP-related proteins as playing important roles in vesicular transport between the endoreticulum and Golgi. Taken together, these results suggest that the VAMP proteins found on synaptic vesicles might represent specialized forms of proteins which participate in general aspects of cell membrane trafficking.