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. 2011 Apr 21;6(4):e18985. doi: 10.1371/journal.pone.0018985

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Ammosova et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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CDK9's Thr186 dephosphorylation by PP1/PIP1 complex leads to the dissociation of 7SK RNA and HEXIM1 protein and the release of inactive CDK9. CDK9 is phosphorylated by a cellular kinase, which may include active CDK9/cyclin T1 on Ser175 and Thr 186 that creates inactive CDK9/cyclin T1. This inactive phosphorylated CDK9/cyclin T1 is activated by PP1/PIP2 complex. The active CDK9/cyclin T1 can be recruited by Tat or re-associated with 7SK snRNP.