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Gene Review

CDK5  -  cyclin-dependent kinase 5

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Disease relevance of CDK5

  • Three truncated forms of p35 including the one corresponding to the 25-kDa subunit of the kinase have been expressed in Escherichia coli and shown to activate a bacteria-expressed Cdk5 with equal efficacy [1].

High impact information on CDK5

  • In vitro, the Cdk5 subunit of NCLK binds to the microtubule-binding region of tau and NCLK associates with microtubules only in the presence of tau [2].
  • Phosphoamino acid and phosphopeptide analysis of the phosphorylated Nclk revealed that Thr-14 of Cdk5 was the sole site of protein phosphorylation [3].
  • Interaction of cyclin-dependent kinase 5 (Cdk5) and neuronal Cdk5 activator in bovine brain [4].
  • When the macromolecular complex was subjected to gel filtration chromatography in the presence of 10% ethylene glycol, the fractions containing both p35nck5a and Cdk5, although eluting at the same position as control, displayed high kinase activity [4].
  • Dephosphorylation kinetics suggest that the PDPK site, but not CKII sites, may negatively regulate the interaction with F-actin [5].

Biological context of CDK5

  • We determined the amino acid sequence of the 30 kDa subunit and found it to be homologous with a cdc2-related kinase, PSSALRE/cdk5 [6].
  • Protein kinase C and MAP kinase inhibitors reduced labeling by about 30%, while CDK5 and CaMK II inhibitors had no effect. cAMP-dependent protein kinase (PKA) inhibitor H89 reduced RGS9-1 labeling by more than 90%, while dibutyryl-cAMP stimulated it 3-fold, implicating PKA as the major kinase responsible for RGS9-1 phosphorylation in OS [7].
  • This study provides the framework for a molecular genetic analysis of CDK5 function [8].
  • Tau protein kinase II (TPKII) is shown by immunoprecipitation to be a complex composed of two subunits, a catalytic subunit, cdk5, and regulatory subunit, p23 [9].
  • Previous studies identified proline-directed protein kinase (PDPK) as a growth factor-sensitive serine/threonine protein kinase that is active in the cytosol of proliferative cells and tissues during interphase [10].

Anatomical context of CDK5

  • The phosphorylation of Nclk by the purified thymus kinase occurred on Cdk5 [3].
  • In this communication, we report that the regulatory subunit (RII) of bovine cardiac muscle cAMP-dependent protein kinase (PKA) is a putative substrate for the multifunctional PDPK [10].

Associations of CDK5 with chemical compounds

  • The production of [33P] phosphorylated peptide is inhibited in the presence of a known TPK II/cdk5 inhibitor but is unaffected in the presence of 1% DMSO [11].


  1. Reconstitution of neuronal Cdc2-like kinase from bacteria-expressed Cdk5 and an active fragment of the brain-specific activator. Kinase activation in the absence of Cdk5 phosphorylation. Qi, Z., Huang, Q.Q., Lee, K.Y., Lew, J., Wang, J.H. J. Biol. Chem. (1995) [Pubmed]
  2. Interaction of neuronal Cdc2-like protein kinase with microtubule-associated protein tau. Sobue, K., Agarwal-Mawal, A., Li, W., Sun, W., Miura, Y., Paudel, H.K. J. Biol. Chem. (2000) [Pubmed]
  3. Demonstration of cyclin-dependent kinase inhibitory serine/threonine kinase in bovine thymus. Matsuura, I., Wang, J.H. J. Biol. Chem. (1996) [Pubmed]
  4. Interaction of cyclin-dependent kinase 5 (Cdk5) and neuronal Cdk5 activator in bovine brain. Lee, K.Y., Rosales, J.L., Tang, D., Wang, J.H. J. Biol. Chem. (1996) [Pubmed]
  5. Dephosphorylated but not phosphorylated microtubule associated protein MAP1B binds to microfilaments. Pedrotti, B., Islam, K. FEBS Lett. (1996) [Pubmed]
  6. A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubule. Kobayashi, S., Ishiguro, K., Omori, A., Takamatsu, M., Arioka, M., Imahori, K., Uchida, T. FEBS Lett. (1993) [Pubmed]
  7. Phosphorylation of the regulator of G protein signaling RGS9-1 by protein kinase A is a potential mechanism of light- and Ca2+-mediated regulation of G protein function in photoreceptors. Balasubramanian, N., Levay, K., Keren-Raifman, T., Faurobert, E., Slepak, V.Z. Biochemistry (2001) [Pubmed]
  8. Cloning and characterization of the Drosophila melanogaster CDK5 homolog. Hellmich, M.R., Kennison, J.A., Hampton, L.L., Battey, J.F. FEBS Lett. (1994) [Pubmed]
  9. Precursor of cdk5 activator, the 23 kDa subunit of tau protein kinase II: its sequence and developmental change in brain. Uchida, T., Ishiguro, K., Ohnuma, J., Takamatsu, M., Yonekura, S., Imahori, K. FEBS Lett. (1994) [Pubmed]
  10. Phosphorylation of RII subunit and attenuation of cAMP-dependent protein kinase activity by proline-directed protein kinase. Braun, R.K., Vulliet, P.R., Carbonaro-Hall, D.A., Hall, F.L. Arch. Biochem. Biophys. (1991) [Pubmed]
  11. A scintillation proximity assay for studying inhibitors of human tau protein kinase II/cdk5 using a 96-well format. Evans, D.B., Rank, K.B., Sharma, S.K. J. Biochem. Biophys. Methods (2002) [Pubmed]
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