@inbook{c566953a07254ad8a8a52a60623df5b9,
title = "Coupling of dephosphorylation and nuclear export of smads in TGF-β signaling",
abstract = "In eukaryotes, regulation of signaling mediators/effectors in the nucleus is one of the principal mechanisms that govern duration and strength of signaling. Smads are a family of structurally related intracellular proteins that serve as signaling effectors for transforming growth factor beta (TGF-β) and TGF-β-related proteins. Accumulating evidence demonstrates that Smads possess intrinsic nucleocytoplasmic shuttling capacity, which enables them to transmit TGF-β signals from cell membrane to nucleus. We recently identified two important steps in the termination of nuclear Smad signaling. The first step is initiated by a serine/threonine phosphatase PPM1A that dephosphorylates Smad2/3 in the nucleus, thereby shutting down signaling capacity of phosphorylated Smad2/3. The second step involves nuclear export of dephosphorylated Smad2/3 with the aid of nuclear protein RanBP3 to terminate Smad signaling. This chapter introduces methods for examining nuclear export of Smad2/3 in TGF-β signaling.",
keywords = "Nuclear export, Nuclear phosphatase, PPM1A, RanBP3, Signal transduction, Smad",
author = "Fangyan Dai and Xueyan Duan and Liang, {Yao Yun} and Xia Lin and Feng, {Xin Hua}",
year = "2010",
doi = "10.1007/978-1-60761-738-9_7",
language = "English (US)",
isbn = "9781607617372",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "125--137",
booktitle = "Transcription Factors",
}