Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6). Keratin 17 is involved in wound healing and cell growth, two processes that require rapid cytoskeletal remodeling (7). Keratinocytes deficient in keratin 17 exhibit abnormal Akt/mTOR signaling and fail to produce an increase in translation, cell size, or growth; these cells also exhibit abnormal 14-3-3σ localization. As 14-3-3σ typically associates with keratin 17, these results imply that Akt/mTOR signaling results in sequestration of 14-3-3σ with keratin 17 in the cytosol, which is required for translation and cell growth. Phosphorylation of keratin 17 on Ser44 may provide a docking site for 14-3-3σ binding (8).