Abstract
We have previously documented that a cellular chaperone protein, FKBP52, which is phosphorylated at both tyrosine and serine/threonine residues, interacts with the D-sequence in the inverted terminal repeats of the adeno-associated virus 2 (AAV) genome, inhibits the viral second-strand DNA synthesis, and leads to inefficient transgene expression from recombinant AAV vectors in certain cell types (J. Virol., 75: 9818-9678, 2001). We have also demonstrated that FKBP52 is dephosphorylated at tyrosine residues by T cell protein tyrosine phosphatase (TC-PTP) (J.
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