@article{88471,
  keywords = {Animals, Humans, signal transduction, Trans-Activators, Protein Binding, HeLa Cells, Receptors, Cytoplasmic and Nuclear, DNA-Binding Proteins, Mice, Peptide Fragments, Cell Nucleus, Cytoplasm, Active Transport, Cell Nucleus, Protein Transport, Transforming Growth Factor beta, 3T3 Cells, COS Cells, Karyopherins, Nuclear Pore, Nuclear Pore Complex Proteins, Smad2 Protein},
  author = {Lan Xu and Yibin Kang and Seda C{\"o}l and Joan Massagu{\'e}},
  title = {Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFbeta signaling complexes in the cytoplasm and nucleus.},
  abstract = {<p>The transcription factor Smad2 is released from cytoplasmic retention by TGFbeta receptor-mediated phosphorylation, accumulating in the nucleus where it associates with cofactors to regulate transcription. We uncovered direct interactions of Smad2 with the nucleoporins CAN/Nup214 and Nup153. These interactions mediate constitutive nucleocytoplasmic shuttling of Smad2. CAN/Nup214 and Nup153 compete with the cytoplasmic retention factor SARA and the nuclear Smad2 partner FAST-1 for binding to a hydrophobic corridor on the MH2 surface of Smad2. TGFbeta receptor-mediated phosphorylation stimulates nuclear accumulation of Smad2 by modifying its affinity for SARA and Smad4 but not for CAN/Nup214 or Nup153. Thus, by directly contacting the nuclear pore complex, Smad2 undergoes constant shuttling, providing a dynamic pool that is competitively drawn by cytoplasmic and nuclear signal transduction partners.</p>
},
  year = {2002},
  journal = {Mol Cell},
  volume = {10},
  pages = {271-82},
  month = {08/2002},
  issn = {1097-2765},
  language = {eng},
}