Pre-TGFB1 complex Large latent complex of TGFB1 Latent TGF-beta-1 is cleaved by furin Authored: Heldin, CH, Moustakas, A, Huminiecki, L, Jassal, B, 2006-02-02 EC Number: 3.4.21 Edited: Jassal, B, 2006-01-18 10:19:52 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. 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) Pubmed12482908 Pubmed7737999 Reactome Database ID Release 43170844 Reactome, http://www.reactome.org ReactomeREACT_6931 Reviewed: Heldin, CH, 2006-04-18 14:26:12 Reviewed: Huang, Tao, 2012-05-14