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• W2006507150 abstract "Smad1, a downstream regulator of the bone morphogenetic protein (BMP) receptors, is tightly regulated by the ubiquitin-proteasomal degradation system. To dissect the mechanisms that underlie the regulation of Smad1, it is important to investigate the specific ubiquitination site(s) in Smad1. Here we report that the α-NH2 group of the N terminus and the ε-NH2 groups of internal lysine residues 116, 118 and 269 (K116, K118 and K269) of Smad1 are ubiquitin acceptor sites mediated by the carboxyl terminus of Hsc70-interacting protein (CHIP). The in vitro degradation assay indicates that ubiquitination at the N terminus partially contributes to the degradation of Smad1. Furthermore, we demonstrate that the ubiquitination level of pseudo-phosphorylated Smad1 by CHIP is stronger than that of wild-type Smad1 and can be strongly inhibited by a phosphorylated tail of Smad1, PIS(pS)V(pS). Third, our results indicate that Hsp70 facilitates CHIP-mediated poly-ubiquitination of Smad1 whereas it attenuates CHIP-meditated mono-ubiquitination of Smad1. Finally, consistent with the in vitro observation, we show that CHIP preferentially mediates the degradation of phospho-Smad1/5 in vivo. Taken together, these results provide us a hint that CHIP might preferentially regulate phosphorylated Smad1 and thus the BMP signaling." @default.
• W2006507150 created "2016-06-24" @default.
• W2006507150 creator A5012268070 @default.
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• W2006507150 creator A5049979053 @default.
• W2006507150 creator A5074200075 @default.
• W2006507150 date "2007-11-01" @default.
• W2006507150 modified "2023-10-13" @default.
• W2006507150 title "Differential Ubiquitination of Smad1 Mediated by CHIP: Implications in the Regulation of the Bone Morphogenetic Protein Signaling Pathway" @default.
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• W2006507150 doi "https://doi.org/10.1016/j.jmb.2007.09.082" @default.
• W2006507150 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17963781" @default.
• W2006507150 hasPublicationYear "2007" @default.
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