Membrane proteases cleave Profilaggrin producing Filaggrin

Stable Identifier
Reaction [transition]
Homo sapiens
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Filaggrin is initially synthesized as a large, insoluble, highly phosphorylated precursor containing many tandem copies of 324 residues. This precursor is dephosphorylated and proteolytically cleaved by several proteases, including the undefined protease PEP1 (Resing et al. 1996), mu-calpain (Yamazaki et al. 1997), furin, PCSK6 (PACE4) (Pearton et al. 2001), PRSS8 (cap1) (Leyvraz et al. 2005), ST14 (matriptase) (List et al. 2003), CELA2 (Bonnart et al. 2010), CASP14 (Denecker et al. 2007) and Kallikrein-related peptidase 5 (KLK5) (Sakabe et al. 2013). Filaggrin is further processed and proteolytically degraded by CASP14 (Eckhart & Tschachler 2011).
Literature References
PubMed ID Title Journal Year
15803139 The cornified envelope: a model of cell death in the skin

Candi, E, Melino, G, Schmidt, R

Nat. Rev. Mol. Cell Biol. 2005
11380615 Proprotein convertase expression and localization in epidermis: evidence for multiple roles and substrates

Dale, BA, Pearton, DJ, Nirunsuksiri, W, Presland, RB, Rehemtulla, A, Lewis, SP

Exp. Dermatol. 2001
16061697 The epidermal barrier function is dependent on the serine protease CAP1/Prss8

Guitard, M, Breiden, B, Rubera, I, Charles, RP, Leyvraz, C, Hummler, E, Sandhoff, K, Rotman, S

J. Cell Biol. 2005
Catalyst Activity

endopeptidase activity of Membrane profilaggrin processing proteases [plasma membrane]

Orthologous Events
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