Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870327 | FEBS Letters | 2014 | 6 Pages |
Abstract
Synaptotagmins are two C2 domain-containing transmembrane proteins. The function of calcium-sensitive members in the regulation of post-Golgi traffic has been well established whereas little is known about the calcium-insensitive isoforms constituting half of the protein family. Novel binding partners of synaptotagmin 11 were identified in β-cells. A number of them had been assigned previously to ER/Golgi derived-vesicles or linked to RNA synthesis, translation and processing. Whereas the C2A domain interacted with the Q-SNARE Vti1a, the C2B domain of syt11 interacted with the SND1, Ago2 and FMRP, components of the RNA-induced silencing complex (RISC). Binding to SND was direct via its N-terminal tandem repeats. Our data indicate that syt11 may provide a link between gene regulation by microRNAs and membrane traffic.
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Authors
Alexandra Milochau, Valérie Lagrée, Marie-Noëlle Benassy, Stéphane Chaignepain, Julien Papin, Itsaso Garcia-Arcos, Anne Lajoix, Carole Monterrat, Laetitia Coudert, Jean-Marie Schmitter, Begoña Ochoa, Jochen Lang,