Reactome | Membrane proteases cleave Profilaggrin producing Filaggrin

Membrane proteases cleave Profilaggrin producing Filaggrin

Stable Identifier

R-HSA-8849797

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol

ReviewStatus

5/5

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Membrane proteases cleave Profilaggrin producing Filaggrin

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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, Schmidt, R, Melino, G	Nat. Rev. Mol. Cell Biol.	2005
11380615	Proprotein convertase expression and localization in epidermis: evidence for multiple roles and substrates Pearton, DJ, Nirunsuksiri, W, Rehemtulla, A, Lewis, SP, Presland, RB, Dale, BA	Exp. Dermatol.	2001
16061697	The epidermal barrier function is dependent on the serine protease CAP1/Prss8 Leyvraz, C, Charles, RP, Rubera, I, Guitard, M, Rotman, S, Breiden, B, Sandhoff, K, Hummler, E	J. Cell Biol.	2005