Latent TGF-beta-1 is cleaved by FURIN

Stable Identifier
Reaction [transition]
Homo sapiens
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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
Catalyst Activity

serine-type endopeptidase activity of FURIN [Golgi membrane]

Orthologous Events
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