Reference work entry
The adaptor protein SARA was first identified as a novel serine protease-like molecule in human brain (Meckelein et al. 1998), and then later characterized as an important regulator of TGF-ß1 signal transduction. SARA interacts with both the type I and type II TGF-ß1 receptors (TßRI and TßRII), and contains a Smad-binding domain (SBD) as well as a double zinc finger FYVE domain that localizes SARA to endosomal subcellular compartments (Tsukazaki et al. 1998). SARA also contains a region homologous to the active site of trypsin-like serine proteases (Meckelein et al. 1998) and a binding motif for the catalytic subunit of type 1 serine/threonine protein phosphatase (PP1c) (Bennett and Alphey 2002). Three alternatively spliced transcripts encoding distinct isoforms have been found for this gene (Fig. 1).
- Liu C, Gaca MD, Swenson ES, Vellucci VF, Reiss M, Wells RG. Smads 2 and 3 are differentially activated by transforming growth factor-beta (TGF-beta) in quiescent and activated hepatic stellate cells. Constitutive nuclear localization of Smads in activated cells is TGF-beta-independent. J Biol Chem. 2003;278(13):11721–8.PubMedPubMedCentralCrossRefGoogle Scholar
- Runyan CE, Schnaper HW, Poncelet AC. The role of internalization in transforming growth factor beta1-induced Smad2 association with Smad anchor for receptor activation (SARA) and Smad2-dependent signaling in human mesangial cells. J Biol Chem. 2005;280(9):8300–8.PubMedPubMedCentralCrossRefGoogle Scholar
- Tao YY, Cui HY, Liu CH. Dynamic characteristics of SARA during liver fibrogenesis in rats. Zhong Gan Zang Bing Za Zhi. 2006;14(12):909–13.Google Scholar
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