title: Cuts by caspase-14 control the proteolysis of filaggrin.
abstract: Although mutations in the filaggrin gene (FLG) have been shown to be associated with ichthyosis vulgaris and atopic dermatitis, the function and regulation of filaggrin remain incompletely understood. In this issue, Hoste et al. report that filaggrin is directly cleaved by caspase-14. Acting in concert with other proteases, caspase-14 controls the breakdown of filaggrin to free amino acids and amino acid derivatives that contribute to the hydration and UVB absorption capacity of the stratum corneum. These findings identify a new layer of complexity in the regulation of epidermal barrier function.
authors: Department of Dermatology, Medical University of Vienna, Vienna, Austria. leopold.eckhart@meduniwien.ac.at
authors: Leopold
authors: L
authors: Eckhart
authors: Erwin
authors: E
authors: Tschachler
mesh_terms: D000818:Animals; D053456:Caspase 14 / Q000378:metabolism*; D005260:Female; D000091344:Filaggrin Proteins; D007381:Intermediate Filament Proteins / Q000378:metabolism*; D059748:Proteolysis; D011761:Pyrrolidonecarboxylic Acid / Q000378:metabolism*; D012867:Skin / Q000378:metabolism*; D014560:Urocanic Acid / Q000378:metabolism*
chemical_list: D000091344:Filaggrin Proteins; D007381:Intermediate Filament Proteins; D053456:Caspase 14; D014560:Urocanic Acid; D011761:Pyrrolidonecarboxylic Acid