TY - JOUR
T1 - Synaptic transmission persists in synaptotagmin mutants of Drosophila
AU - DiAntonio, Aaron
AU - Parfitt, Karen D.
AU - Schwarz, Thomas L.
N1 - Funding Information:
We wish to thank Jeff Sekelsky, Bill Gelbart, and Bruce Baker for providing us with Drosophila stocks, Beverly Wendland and Ken Miller for the gift of their affinity purified anti-synaptotagmin antisera, Felix Schweizer for the data acquisition software, and Kendal Broadie for advice on embryo cultures and recordings. We also wish to thank Irene lnman for excellent technical assistance and Robert Burgess, David Deitcher, and Noreen Reist for discussions and for comments on this manuscript. This work was supported by the McKnight Foundation and a Silvio Conti Center for Neuroscience Award from the National Institute of Mental Health (NIMH). A. D. was supported by a Medical Scientist Training Program fellowship from the National Institute of General Medical Sciences (5T32 GM07365). K. D. P. was supported by a National Research Service Award from the NIMH.
PY - 1993/7/2
Y1 - 1993/7/2
N2 - Synaptotagmin is one of the major integral membrane proteins of synaptic vesicles. It has been postulated to dock vesicles to their release sites, to act as the Ca2+ sensor for the release process, and to be a fusion protein during exocytosis. To clarify the function of this protein, we have undertaken a genetic analysis of the synaptotagmin gene in Drosophila. We have Identified five lethal alleles of synaptotagmin, at least one of which lacks detectable protein. Surprisingly, however, many embryos homozygous for this null allele hatch and, as larvae, crawl, feed, and respond to stimuli. Electrophysiological recordings in embryonic cultures confirmed that synaptic transmission persists in the null allele. Therefore, synaptotagmin is not absolutely required for the regulated exocytosis of synaptic vesicles. The lethality of synaptotagmin in late first instar larvae is probably due to a perturbation of transmission that leaves the main apparatus for vesicle docking and fusion intact.
AB - Synaptotagmin is one of the major integral membrane proteins of synaptic vesicles. It has been postulated to dock vesicles to their release sites, to act as the Ca2+ sensor for the release process, and to be a fusion protein during exocytosis. To clarify the function of this protein, we have undertaken a genetic analysis of the synaptotagmin gene in Drosophila. We have Identified five lethal alleles of synaptotagmin, at least one of which lacks detectable protein. Surprisingly, however, many embryos homozygous for this null allele hatch and, as larvae, crawl, feed, and respond to stimuli. Electrophysiological recordings in embryonic cultures confirmed that synaptic transmission persists in the null allele. Therefore, synaptotagmin is not absolutely required for the regulated exocytosis of synaptic vesicles. The lethality of synaptotagmin in late first instar larvae is probably due to a perturbation of transmission that leaves the main apparatus for vesicle docking and fusion intact.
UR - http://www.scopus.com/inward/record.url?scp=0027180569&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(93)90356-U
DO - 10.1016/0092-8674(93)90356-U
M3 - Article
C2 - 8100740
AN - SCOPUS:0027180569
SN - 0092-8674
VL - 73
SP - 1281
EP - 1290
JO - Cell
JF - Cell
IS - 7
ER -