TY - JOUR
AU - Massagué, Joan
AB - brief communications The nuclear import function of Smad2 is masked by SARA and unmasked by TGFb b b b- dependent phosphorylation Lan Xu*, Ye-Guang Chen* and Joan Massagué*† *Cell Biology Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA †e-mail: j-massague@ski.mskcc.org uclear accumulation of Smad transcription factors in response (WGA), which prevents active transport, but not free diffusion, 5,7,8 to transforming growth factor b CTGFb cytokines is triggered across the nuclear membrane , blocked nuclear import of GST– by TGFb-receptor-mediated phosphorylation . Receptor MH2 and of GST–MH2+L (Fig. 1b and data not shown). phosphorylation of Smad2, which occurs in the extreme carboxy- These results are consistent with the previous finding that a terminal sequence SSMS, allows association of this protein with the fusion of the Smad2 MH2 domain with b-galactosidase is constitu- related protein Smad4. Smad4 is important for assembly of tran- tively accumulated in nuclei in Xenopus embryos . We also found scriptional complexes, but is not required for nuclear that, when fused to green fluorescent protein (GFP), the MH2 accumulation . The mechanism by which receptor-mediated phos- domain, but not the MH1 domain, is constitutively accumulated in phorylation promotes nuclear 
TI - The nuclear import function of Smad2 is masked by SARA and unmasked by TGFb-dependent phosphorylation
JF - Nature Cell Biology
DO - 10.1038/35019649
DA - 2000-07-19
UR - https://www.deepdyve.com/lp/springer-journals/the-nuclear-import-function-of-smad2-is-masked-by-sara-and-unmasked-by-4aESQS7smG
SP - 559
EP - 562
VL - 2
IS - 8
DP - DeepDyve
ER -