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The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins

Article Abstract:

Phosphorylation of mitotic proteins on the Ser/Thr-Pro motifs is a significant factor in regulating mitotic progression. The necessary mitotic peptidyl-prolyl isomerase Pin1 regulates mitosis-specific phosphoproteins and binds them. In human cells and Xenopus extracts, Pin1 is involved directly with a subset of mitotic phosphoproteins on phosphorylated Ser/Thr-Pro patterns in a phosphorylation-dependent and mitosis-specific way.

Cell cycle, Mitosis, Phosphoproteins, Isomerases

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Pin1 modulates RNA polymerase II activity during the transcription cycle

Article Abstract:

The roles played by Pin1 in modulating the RNA polymerase II (RNAP II) transcription are examined. Chromatin immunoprecipitation (ChIP) shows that the inhibition has reflected Pin1 activity during transcription initiation and not elongation, indicating that Pin1 modulated the C-terminal domain of RNAP II largest subunit (CTD) phosphorylation, and RNAP II activity, during an early stage of transcription cycle.

Chromatin, Genetic transcription, Transcription (Genetics)

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Pin 1 modulates the structure and function of human RNA polymerase II

Article Abstract:

The influence of peptidyl-prolyl isomerase Pin1 on the phosphorylation status of the C-terminal domain (CTD) in vitro is shown by inhibiting the CTD phosphatase FCP1 and stimulating CTD phosphorylation by cdc2/cyclin B. thus, a significant role is played by Pin1 in regulating RNAP II CTD structure and function.

Influence, Cyclophilin, Genetic research, Properties, Structure

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