| Literature DB >> 20694664 |
Fangyan Dai1, Xueyan Duan, Yao-Yun Liang, Xia Lin, Xin-Hua Feng.
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-beta) and TGF-beta-related proteins. Accumulating evidence demonstrates that Smads possess intrinsic nucleocytoplasmic shuttling capacity, which enables them to transmit TGF-beta 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-beta signaling.Entities:
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Year: 2010 PMID： 20694664 PMCID： PMC3153448 DOI： 10.1007/978-1-60761-738-9_7
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745