The dataset of proteins specifically interacted with activated TICAM-1
Kenji Funami,
Misako Matsumoto,
Hiroyuki Oshiumi,
Chikashi Obuse,
Tsukasa Seya
Affiliations
Kenji Funami
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan; Corresponding authors.
Misako Matsumoto
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan
Hiroyuki Oshiumi
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan; Division of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan
Chikashi Obuse
Division of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan
Tsukasa Seya
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan; Corresponding authors.
The presented data are related with our paper entitled “14-3-3-zeta participates in TLR3-mediated TICAM-1 signal-platform formation” (Funami et al., 2016) [1]. These data show the proteins which specifically bind to the activated (oligomerized) TICAM-1. Fifty-three proteins were identified as specifically interacted with oligomerized TICAM-1. Mutant TICAM-1 cannot form the active oligomer, so the proteins interacted with mutant TICAM-1 are dispensable for TICAM-1-signaling. Among 53 proteins, 14-3-3-zeta specifically interacts with oligomerized TICAM-1 to corroborate TICAM-1 signalosome. Keywords: TLR3, TICAM-1 (TRIF), 14-3-3, Signalosome, Proteome analysis
