Open AccessIdentification of a Smad Phosphatase
Author(s) -
Caroline S. Hill
Publication year - 2006
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb6002702
Subject(s) - smad , phosphatase , phosphorylation , signal transduction , microbiology and biotechnology , superfamily , biology , smad2 protein , chemistry , receptor , biochemistry
Activation of Smad signaling pathways downstream of TGF-beta superfamily ligands via receptor-mediated Smad phosphorylation is well understood, but little is known about the phosphatases that turn off Smad activity. Now in Cell, Feng and colleagues (Lin, X., et al. (2006) Cell 125 , 915-928) report their discovery that PPM1A acts as a Smad phosphatase to terminate TGF-beta signaling.