PMID: 11918675Mar 29, 2002Paper

The FYVE domain in Smad anchor for receptor activation (SARA) is sufficient for localization of SARA in early endosomes and regulates TGF-beta/Smad signalling

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
Fumiko ItohPeter ten Dijke Pt

Abstract

Transforming growth factor-beta (TGF-beta) initiates intracellular signalling by inducing the formation of a heteromeric complex between TGF-beta type I (TbetaR-I) and TGF-beta type II serine/threonine kinase receptors (TbetaR-II). After the activation of TbetaR-I kinase by TbetaR-II kinase, specific receptor-regulated Smads (R-Smads) are phosphorylated by TbetaR-I kinase. Smad anchor for receptor activation (SARA), which contains a FYVE finger domain, regulates the subcellular localization of R-Smads and presents them to TbetaR-I. However, it is unclear where SARA is localized in the cell and which phospholipid(s) interacts with its FYVE domain. Wild-type SARA and the FYVE domain of SARA (FYVE(SARA)) reveal a punctate staining pattern and co-localize with the early endosomal markers, early endosomal antigen-1 (EEA1) and hepatic growth factor-regulated tyrosine kinase substrate (Hrs). The ectopic expression of dominant negative rab5, a critical regulatory molecule in endosome function, redistributes SARA from punctate to a diffuse cytosolic staining pattern. A lipid binding assay demonstrated that the recombinant FYVE domain from SARA predominantly interacts with phosphatidylinositol 3-phosphate (PtdIns(3)P). Consistent with th...Continue Reading

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