LTBP4 binds TGF-Beta-1

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Transforming growth factor (TGF) beta (TGF-beta) is a family of three cytokine 'isoforms' (encoded by three separate human genes) that control proliferation, cellular differentiation and other functions. TGF-beta originally referred to the founding member TGF-beta-1, now it is often used as a collective term for all three. TGF-beta is secreted from cells in latent form as part of a complex that includes two other proteins: the cleaved propeptide of TGF beta, known as latency associated peptide (LAP), and a member of the latent TGF beta binding protein (LTBP) family. LTBPs are members of the fibrillin/LTBP superfamily, characterised by the presence of unique TGF-binding protein (TB) domains, also known as 8 cys domains as they contain eight characteristic cysteines (Ramirez & Sakai 2010). LTBPs are microfibril-associated, proteins that tether latent complexes of TGF-beta to microfibrils in the ECM (Taipale et al. 1996, Dallas et al. 2000, Isogai et al. 2003, Hyytiainen et al. 2004, Ono et al. 2009, Munger & Sheppard 2011). LTBP1 and 3 bind all three isoforms of latent TGF-beta, while LTBP4 only weakly binds TGF-beta1 (Saharinen & Keski Oja 2000). LTBP2 does not bind TGF-beta and is a structural component of fibrillin microfibrils. The carboxyl terminus of LTBP1 binds to fibrillin-1. LTBP1 and LTBP4 incorporation into the ECM is abolished in fibrillin-1 null mice (Ono et al. 2009). The amino terminus of LTBPs binds ECM components such as collagen (Taipale et al. 1996) and fibronectin (Kantola et al. 2008). Fibulins compete for the LTBP sites in fibrillin (Ono et al. 2009).

Literature References
PubMed ID Title Journal Year
12429738 Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein

Sakai, LY, Rifkin, DB, Isogai, Z, Mazzieri, R, Chen, Y, Ono, RN, Keene, DR, Charbonneau, NL, Ushiro, S, Reinhardt, DP

J. Biol. Chem. 2003
Orthologous Events
Cite Us!