Latent TGF-beta-1 is cleaved by furin

Stable Identifier
R-HSA-170844
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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. 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)

Literature References
PubMed ID Title Journal Year
12482908 Making sense of latent TGFbeta activation

Annes, JP, Munger, JS, Rifkin, DB

J Cell Sci 2003
7737999 Processing of transforming growth factor beta 1 precursor by human furin convertase

Dubois, CM, Laprise, MH, Blanchette, F, Gentry, LE, Leduc, R

J Biol Chem 1995
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
serine-type endopeptidase activity of FURIN [Golgi membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created