The long form of CDK2 arises via alternative splicing and forms an active protein kinase with cyclins A and E

Claudia Ellenrieder, Birke Bartosch, Yuan-Chii Gladys Lee, Martin Murphy, Claire Sweeney, Martin Hergersberg, Mark Carrington, Rolf Jaussi, Tim Hunt

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We have reinvestigated the long form of cyclin-dependent kinase (CDK)2 that is expressed in many rodent cells. We show that the mRNA encoding CDK2L arises by alternative splicing and that the encoded protein can bind to, and be activated by, cyclins A and E. The complex of CDK2L with cyclin A has about half the specific activity of the equivalent CDK2-cyclin A complex. Also, CDK2L-cyclin A is inhibited to the same extent and by the same concentrations of p21CIP1 as CDK2-cyclin A. The nucleotide sequences of intron V in the human and murineCDK2 genes, where the sequences encoding the 48-residue insert in CDK2L are located, show very high conservation in the position of the alternatively spliced exon and its surroundings. Despite this, we were not able to detect significant expression of CDK2L in human cell lines, although a low level is expressed in COS-1 cells from monkeys.

Original languageEnglish
Pages (from-to)413-423
Number of pages11
JournalDNA and Cell Biology
Volume20
Issue number7
DOIs
Publication statusPublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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    Ellenrieder, C., Bartosch, B., Lee, Y-C. G., Murphy, M., Sweeney, C., Hergersberg, M., Carrington, M., Jaussi, R., & Hunt, T. (2001). The long form of CDK2 arises via alternative splicing and forms an active protein kinase with cyclins A and E. DNA and Cell Biology, 20(7), 413-423. https://doi.org/10.1089/104454901750361479