TICAM2 has been shown to undergo phosphorylation on Ser-16 by protein kinase C (PKC) epsilon in LPS-treated human THP1 and murine embryonic fibroblasts (MEF) cells (McGettrick AF et al. 2006). The phosphorylation at Ser-16 by PKC epsilon was required for TICAM2 to be depleted from the membrane (McGettrick AF et al. 2006).
It has recently been demonstrated that phosphorylation of TICAM2 at tyrosine residue Y167 by an unknown protein tyrosine kinase is needed for TICAM2 translocation from the plasma membrane to the endosomal membrane, where it can associate with the activated TLR4 complex (Huai et al. 2015). PTPN4, a protein tyrosine phosphatase, dephosphorylates Y167 of TICAM2, thus inhibiting TICAM2 endocytosis (Huai et al. 2015).
Akashi-Takamura, S, Matsumoto, F, Miyake, K, Tanimura, N, Saitoh, S
Zhao, J, Huai, W, Li, B, Song, H, Jiang, G, Zhang, L, Zhao, W, Wang, L, Han, L, Gao, C
Fitzgerald, KA, O'Neill, LA, Palsson-McDermott, EM, Brint, EK, Rowe, DC, Gay, NJ, Golenbock, DT, McGettrick, AF
Horng, T, Kagan, JC, Su, T, Akira, S, Chow, A, Medzhitov, R
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