PT  - JOURNAL ARTICLE
ED  - , 
TI  - Microtubules Regulate Signaling
AID  - 10.1126/stke.2000.18.tw2
DP  - 2000 Feb 08
TA  - Science's STKE
PG  - tw2--tw2
VI  - 2000
IP  - 18
4099  - http://stke.sciencemag.org/content/2000/18/tw2.short
4100  - http://stke.sciencemag.org/content/2000/18/tw2.full
SO  - Sci. STKE2000 Feb 08; 2000
AB  - Signaling by transforming growth factor-β(TGF-β) through the TGF-β2/ TGF-β1 receptor heteroligomer leads to phosphorylation of Smad proteins 2 and 3, which then bind to Smad4 and are translocated to the nucleus and regulate transcription. Dong et al. demonstrated that endogenous Smad2, 3, and 4 colocalize and coimmunoprecipitate with microtubules. Further characterization of the Smad2 interaction showed that TGF-β caused dissociation of Smad2 from microtubules. Drugs that disrupt microtubules caused release of Smad2 from microtubules, increased phosphorylation of Smad2, and increased activation of reporter genes with TGF-β-responsive promoters in both TGF-β-treated and untreated cells. Microtubules may serve as negative regulators of TGF-β signaling by controlling the availability of Smad proteins for interaction with the TGF-β receptor. Dong, C., Li, Z., Alvarez Jr., R., Feng, X.-H., Goldschmidt-Clermont, P.J. (2000) Microtubule binding to Smads may regulate TGFβ activity. Mol. Cell 5: 27-34. [Online Journal]