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    J Biol Chem. 2003 Jan 3;278(1):428-37. Epub 2002 Oct 21.

    SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1.

    Raju GP, Dimova N, Klein PS, Huang HC.

    Source

    Cell & Molecular Biology Graduate Group, University of Pennsylvania Medical Center, Philadelphia, Pennsylvania 19104, USA.

    Abstract

    Bone morphogenetic proteins (BMPs) are members of the transforming growth factor-beta (TGF-beta) superfamily that play important roles in bone formation, embryonic patterning, and epidermal-neural cell fate decisions. BMPs signal through pathway specific mediators such as Smads1 and 5, but the upstream regulation of BMP-specific Smads has not been fully characterized. Here we report the identification of SANE (Smad1 Antagonistic Effector), a novel protein with significant sequence similarity to nuclear envelop proteins such as MAN1. SANE binds to Smad1/5 and to BMP type I receptors and regulates BMP signaling. SANE specifically blocks BMP-dependent signaling in Xenopus embryos and in a mammalian model of bone formation but does not inhibit the TGF-beta/Smad2 pathway. Inhibition of BMP signaling by SANE requires interaction between SANE and Smad1, because a SANE mutant that does not bind Smad1 does not inhibit BMP signaling. Furthermore, inhibition appears to be mediated by inhibition of BMP-induced Smad1 phosphorylation, blocking ligand-dependent nuclear translocation of Smad1. These studies define a new mode of regulation for intracellular BMP/Smad1 signaling.

    PMID:
    12393873
    [PubMed - indexed for MEDLINE]
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