Membrane proteases cleave Profilaggrin producing Filaggrin

Stable Identifier
R-HSA-8849797
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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
15803139 The cornified envelope: a model of cell death in the skin

Candi, E, Schmidt, R, Melino, G

Nat. Rev. Mol. Cell Biol. 2005
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
endopeptidase activity of Membrane profilaggrin processing proteases [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created