Reactome | TWEAK binds FN14

TWEAK binds FN14

Stable Identifier

R-HSA-5669023

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane, extracellular region

Synonyms

TNFSF12 binds TNFRSF12A

ReviewStatus

5/5

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The cytokine tumor necrosis factor-like weak inducer of apoptosis (TWEAK or TNFSF12) is a member of the TNF superfamily (TNFSF) that contribute to acute kidney injury (AKI) and chronic kidney disorder (CKD), where it has been shown to regulate cell death, inflammation, and fibrosis through activation of the TWEAK receptor fibroblast growth factor-inducible 14 (FN14 or TNFRSF12A). FN14 (TNFRSF12A) is a type I transmembrane and the smallest member of the TNF receptor super family. TWEAK mediates NF-kappaB activation to promote angiogenesis and the proliferation of endothelial cells via its binding to FN14 (TNFSF12A) (Poveda et al. 2013, Lynch et al. 1999, Wiley et al. 2001, Wiley & Winkles 2003). Both membrane bound and soluble forms of TWEAK form homotrimers and have been shown to be able to bind to three monomers of receptor FN14 and trigger signalling (Roos et al. 2010).

Literature References

PubMed ID	Title	Journal	Year
12787562	TWEAK, a member of the TNF superfamily, is a multifunctional cytokine that binds the TweakR/Fn14 receptor Wiley, SR, Winkles, JA	Cytokine Growth Factor Rev.	2003
11728344	A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis Fanslow, WC, Liu, H, Davis-Smith, T, Lofton, T, Lindner, V, Winkles, JA, Wiley, SR, Smith, CA, Daniel, TO, Cassiano, L	Immunity	2001
20385556	Full-length, membrane-anchored TWEAK can function as a juxtacrine signaling molecule and activate the NF-kappaB pathway Ghosh, A, Winkles, JA, Brown, SA	J. Biol. Chem.	2010
23667509	Crystal structure of human TWEAK in complex with the Fab fragment of a neutralizing antibody reveals insights into receptor binding Kohnert, U, Niewoehner, J, Lammens, A, Hopfner, KP, Schraeml, M, von Proff, L, Lammens, K, Baehner, M	PLoS ONE	2013
10085077	TWEAK induces angiogenesis and proliferation of endothelial cells Leal, JA, Lynch, CN, Wang, YC, Wiley, SR, Lund, JK, Chen, YW	J. Biol. Chem.	1999
19241374	Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily Güntert, P, Kobayashi, N, Saito, K, Watanabe, S, Kigawa, T, Tanaka, A, He, F, Muto, Y, Yokoyama, S, Dang, W	Protein Sci.	2009