SMAD7 binds to SMURF1

Stable Identifier
Reaction [binding]
Homo sapiens
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SMAD7 binds to SMURF1 in the nucleus (Ebisawa et al. 2001, Tajima et al. 2003). SMURF1 domains WW1 and WW2, highly similar to WW2 and WW3 domains of SMURF2, are involved in SMAD7 binding. SMURF1 has two splicing isoforms. The shorter splicing isoform of SMURF1 has an inter-WW domain linker of the same length as the WW2-WW3 domain linker of SMURF2. The longer isoform of SMURF1 has a longer WW1-WW2 domain linker, resulting in decreased affinity of the longer SMURF1 isoform for SMAD7 (Chong et al. 2010). This is based on experiments with recombinant mouse Smad7 and recombinant human SMURF1.

Literature References
PubMed ID Title Journal Year
11278251 Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation

Tanaka, K, Chiba, T, Miyazono, K, Murakami, G, Fukuchi, M, Ebisawa, T, Imamura, T

J Biol Chem 2001
12519765 Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-beta signaling by Smad7

Yoshida, M, Miyazono, K, Yoneda, Y, Tajima, Y, Shinomiya, K, Goto, K, Sekimoto, T, Imamura, T

J Biol Chem 2003
20937913 Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity

Wrana, JL, Lin, H, Chong, PA, Forman-Kay, JD

Proc Natl Acad Sci U S A 2010
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