Reactome | Latent TGF-beta-1 is cleaved by FURIN

Latent TGF-beta-1 is cleaved by FURIN

Stable Identifier

R-HSA-170844

Type

Reaction [transition]

Species

Homo sapiens

Compartment

Golgi membrane, Golgi lumen

ReviewStatus

5/5

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In the Golgi apparatus, TGF-beta-1 (TGFB1) is activated by furin protease cleavage of the N-terminal pro-peptide portion. This leads to the formation of the N-terminal disulphide-linked dimeric pro-peptides, also known as latency-associated proteins (LAPs) and the C-terminal mature disulphide-linked dimeric TGF-beta-1 (Dubois et al. 1995, Dubois et al. 2001, Leitlein et al. 2001). However, the N- and C-terminal polypeptides do not physically separate. Rather they stay in one complex. In addition, the LAP forms disulphide links with separate secreted proteins, the Latent TGF-beta binding proteins (LTBPs). LTBPs-linked to LAP and the non-covalently linked mature TGF-beta-1 remain together and form the large latent complex (LLC) (Annes et al. 2003).

Literature References

PubMed ID	Title	Journal	Year
7737999	Processing of transforming growth factor beta 1 precursor by human furin convertase Leduc, R, Blanchette, F, Dubois, CM, Laprise, MH, Gentry, LE	J Biol Chem	1995
12482908	Making sense of latent TGFbeta activation Annes, JP, Rifkin, DB, Munger, JS	J Cell Sci	2003
11390472	Processing of immunosuppressive pro-TGF-beta 1,2 by human glioblastoma cells involves cytoplasmic and secreted furin-like proteases Platten, M, Aulwurm, S, Waltereit, R, Leitlein, J, Wagenknecht, B, Garten, W, Naumann, U, Weller, M	J Immunol	2001
11141505	Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme Laprise, MH, Blanchette, F, Dubois, CM, Grondin, F, Seidah, NG, Leduc, R	Am J Pathol	2001