Abstract
The molecular chaperone αB-crystallin interacts with cytoskeletal structure in the cell. The cytoskeletal component tubulin/microtubule commonly allows the cell to respond mechanically to the environment, and the concentration of free tubulin dimer is autoregulated in the balance if free dimer and polymeric forms of microtubule protein, having an intrinsic property of "dynamic instability." To explore casual relation ships between the αB-crystallin and cytoskeletal structure, we examined tubulin changes that were related to αB-crystallin in rat soleus muscle extracts, and mouse C2C12 clutured muscle cells. The molecular chaperon αB-crystallin seems to play a roll to maintain tubulin and microtubule network appropriately in the gravitational circumstance.
