|
  
- 积分
- 0
- 威望
- 0
- 包包
- 3465
|
.
7 g, p; ^/ e6 c' ^5 N/ [0 m3 ]- U' A+ k+ }, v* L+ \
Cofractionation experiments showed that ?-catenin that interacts with cadherin is in a heterodimer with -catenin, but Wnt signaling induces a monomeric form of ?-catenin that interacts with a transcription factor complex. After enriching for cadherins, ?-catenin can be detected using antibodies to either NH2-terminal or COOH-terminal regions; but in the cadherin-free fraction only the NH2-terminal antibody binds. The team hypothesizes that the ?-catenin protein is folded back on itself in its monomeric form and, as such, is available for transcription complex binding but not for adhesion duties." R. G) a) G8 W! c5 u9 Y
* J! F/ k7 Q# gGottardi speculates that a post-translational modification is responsible for the conformational change but does not yet know what that modification is. Furthermore, she thinks this sort of molecular segregation may be a common mechanism cells use to allow one protein to do multiple jobs, without the more common function soaking up all the protein required for a temporally regulated one.(The cytoplasmic protein ?-catenin is ess) |
|
发表于 2009-3-6 08:14
发表于 2015-5-28 13:27
