Synaptotagmin 11 interacts with components of the RNA-induced silencing complex RISC in clonal pancreatic β-cells

Synaptotagmins are two C-2 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 beta-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. Structured summary of protein interactions: Syt11C2A physically interacts with Vti1a by pull down (View interaction) Syt11C2B physically interacts with SND1, PDIA6, Vti1b, Vti1a, Ago2 and FMRP by pull down (View interaction) syt11C2B binds to SND1 by filter binding (View interaction) Syt11C2B physically interacts with EIF3A, PDIA6, NPM1, EIF3B, NCL, RS3, RS3A, CBR1, ANP32B, LOC683961, SET, SND1, IBB2C, RS10 and RS18 by pull down (View interaction) SND1 physically interacts with Ago2 by anti bait coip (View interaction) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.