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. 2012 Apr 18:7:12.
doi: 10.1186/1747-1028-7-12.

Cyclin K goes with Cdk12 and Cdk13

Jiri Kohoutek  1 , Dalibor Blazek
Affiliations

Cyclin K goes with Cdk12 and Cdk13

Jiri Kohoutek et al. Cell Div. .

Abstract

The cyclin-dependent kinases (Cdks) regulate many cellular processes, including the cell cycle, neuronal development, transcription, and posttranscriptional processing. To perform their functions, Cdks bind to specific cyclin subunits to form a functional and active cyclin/Cdk complex. This review is focused on Cyclin K, which was originally considered an alternative subunit of Cdk9, and on its newly identified partners, Cdk12 and Cdk13. We briefly summarize research devoted to each of these proteins. We also discuss the proteins' functions in the regulation of gene expression via the phosphorylation of serine 2 in the C-terminal domain of RNA polymerase II, contributions to the maintenance of genome stability, and roles in the onset of human disease and embryo development.

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Figures

Figure 1
Figure 1
Domain composition of CycK, Cdk12, and Cdk13. A) A schematic representation of the CycK domain structure. Two cyclin boxes are depicted with a yellow and green ellipse, and the proline-rich domain by a violet oval. B) Schematic diagrams of Cdk12 and Cdk13 domain structures. Putative or verified nuclear localization signals (NLS) are depicted by asterisks. Arginine/serine-rich (RS), proline-rich (PRM), alanine-rich (A), and serine-rich (SR) domains are indicated by orange, green, violet, and purple ovals, respectively. A yellow asterisk represents the kinase domain (KD). Numbers below the schemes indicate the amino acid position for a given domain.
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