Phosphorylation of the beta1 integrin cytoplasmic domain: toward an understanding of function and mechanism.

@article{Mulrooney2000PhosphorylationOT,
  title={Phosphorylation of the beta1 integrin cytoplasmic domain: toward an understanding of function and mechanism.},
  author={James P. Mulrooney and K Foley and Sabrina Vineberg and Mark Barreuther and Laura B. Grabel},
  journal={Experimental cell research},
  year={2000},
  volume={258 2},
  pages={332-41}
}
As F9 stem cells differentiate into parietal endoderm they form focal adhesion sites. There is a concomitant decrease in the level of phosphorylation of S785 in the cytoplasmic domain of the beta1 integrin subunit. Previous transfection studies demonstrate that site-specific mutations at this residue, mimicking different phosphorylation states, can alter the subcellular localization of the subunit in differentiating F9 cells. We now extend these observations in an attempt to substantiate the… CONTINUE READING

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