TY - JOUR
T1 - The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis
AU - MacDougall, Daniel D.
AU - Lin, Zesen
AU - Chon, Nara L.
AU - Jackman, Skyler L.
AU - Lin, Hai
AU - Knight, Jefferson D.
AU - Anantharam, Arun
N1 - Publisher Copyright:
© 2018 MacDougall et al.
PY - 2018/6/1
Y1 - 2018/6/1
N2 - Synaptotagmin (Syt) proteins comprise a 17-member family, many of which trigger exocytosis in response to calcium. Historically, most studies have focused on the isoform Syt-1, which serves as the primary calcium sensor in synchronous neurotransmitter release. Recently, Syt-7 has become a topic of broad interest because of its extreme calcium sensitivity and diversity of roles in a wide range of cell types. Here, we review the known and emerging roles of Syt-7 in various contexts and stress the importance of its actions. Unique functions of Syt-7 are discussed in light of recent imaging, electrophysiological, and computational studies. Particular emphasis is placed on Syt-7-dependent regulation of synaptic transmission and neuroendocrine cell secretion. Finally, based on biochemical and structural data, we propose a mechanism to link Syt-7's role in membrane fusion with its role in subsequent fusion pore expansion via strong calcium-dependent phospholipid binding.
AB - Synaptotagmin (Syt) proteins comprise a 17-member family, many of which trigger exocytosis in response to calcium. Historically, most studies have focused on the isoform Syt-1, which serves as the primary calcium sensor in synchronous neurotransmitter release. Recently, Syt-7 has become a topic of broad interest because of its extreme calcium sensitivity and diversity of roles in a wide range of cell types. Here, we review the known and emerging roles of Syt-7 in various contexts and stress the importance of its actions. Unique functions of Syt-7 are discussed in light of recent imaging, electrophysiological, and computational studies. Particular emphasis is placed on Syt-7-dependent regulation of synaptic transmission and neuroendocrine cell secretion. Finally, based on biochemical and structural data, we propose a mechanism to link Syt-7's role in membrane fusion with its role in subsequent fusion pore expansion via strong calcium-dependent phospholipid binding.
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U2 - 10.1085/jgp.201711944
DO - 10.1085/jgp.201711944
M3 - Review article
C2 - 29794152
AN - SCOPUS:85048084587
SN - 0022-1295
VL - 150
SP - 783
EP - 807
JO - Journal of General Physiology
JF - Journal of General Physiology
IS - 6
ER -