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. 2004 Jan 8;41(1):85-99.
doi: 10.1016/s0896-6273(03)00820-1.

N-glycosylation is essential for vesicular targeting of synaptotagmin 1

Weiping Han  1 , Jeong-Seop Rhee, Anton Maximov, Ye Lao, Tomoyuki Mashimo, Christian Rosenmund, Thomas C Südhof
Affiliations
Free article

N-glycosylation is essential for vesicular targeting of synaptotagmin 1

Weiping Han et al. Neuron. .
Free article

Abstract

Synaptotagmins 1 and 7 are candidate Ca(2+) sensors for exocytosis localized to synaptic vesicles and plasma membranes, respectively. We now show that the N-terminal intraluminal sequence of synaptotagmin 1, when transplanted onto synaptotagmin 7, redirects synaptotagmin 7 from the plasma membrane to secretory vesicles. Conversely, mutation of the N-terminal N-glycosylation site of synaptotagmin 1 redirects synaptotagmin 1 from vesicles to the plasma membrane. In cultured hippocampal neurons, the plasma membrane-localized mutant of synaptotagmin 1 suppressed the readily releasable pool of synaptic vesicles, whereas wild-type synaptotagmin 1 did not. In addition to the intraluminal N-glycosylation site, the cytoplasmic C(2) domains of synaptotagmin 1 were required for correct targeting but could be functionally replaced by the C(2) domains of synaptotagmin 7. Our data suggest that the intravesicular N-glycosylation site of synaptotagmin 1 collaborates with its cytoplasmic C(2) domains in directing synaptotagmin 1 to synaptic vesicles via a novel N-glycosylation-dependent mechanism.

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