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- Title
Dermokine-β impairs ERK signaling through direct binding to GRP78
- Authors
Higashi, Kiyoshi; Hasegawa, Minoru; Yokoyama, Chikako; Tachibana, Taro; Mitsui, Shinichi; Saito, Koichi
- Abstract
Abstract: Dermokine-β is abundant in stratified epithelia and in differentiating cultured keratinocytes. In this study, we investigated the role of dermokine-β in differentiation of keratinocytes. Treatment of keratinocytes or skin tumor cells with dermokine-β attenuated phosphorylation of extracellular-signal-regulated kinase (ERK). Exposure of cells to dermokine-β, as well as its carboxyl-terminus domain peptide, interrupted phosphorylation of ERK and stimulated dermokine gene expression. Inhibition of ERK signaling by its specific inhibitor also increased dermokine expression level. A combination of chemical cross-linking and immunoprecipitation, followed by proteomics analyses, identified glucose-regulated protein 78 (GRP78) as a dermokine-β-associated protein. Blockage of GRP78 expression by a specific siRNA abrogated actions of dermokine-β. These findings provide novel insights into the physiological significance of dermokine-β in the epidermis. Structured summary of protein interactions: dermokine-Beta physically interacts with GRP78 by cross-linking study (View interaction) dermokine-Beta(Glo2) and GRP78 physically interact by competition binding (View interaction) dermokine-Beta binds to GRP78 by anti bait coimmunoprecipitation (View interaction)
- Subjects
CELLULAR signal transduction; EPITHELIAL cells; CELL culture; KERATINOCYTES; CANCER cells; PHOSPHORYLATION; PROTEOMICS
- Publication
FEBS Letters, 2012, Vol 586, Issue 16, p2300
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2012.06.022