The C-terminal tail of protein kinase D2 and protein kinase D3 regulates their intracellular distribution

Biochem Biophys Res Commun. 2006 Apr 14;342(3):685-9. doi: 10.1016/j.bbrc.2006.02.013. Epub 2006 Feb 13.

Abstract

We generated a set of GFP-tagged chimeras between protein kinase D2 (PKD2) and protein kinase D3 (PKD3) to examine in live cells the contribution of their C-terminal region to their intracellular localization. We found that the catalytic domain of PKD2 and PKD3 can localize to the nucleus when expressed without other kinase domains. However, when the C-terminal tail of PKD2 was added to its catalytic domain, the nuclear localization of the resulting protein was inhibited. In contrast, the nuclear localization of the CD of PKD3 was not inhibited by its C-terminal tail. Furthermore, the exchange of the C-terminal tail of PKD2 and PKD3 in the full-length proteins was sufficient to exchange their intracellular localization. Collectively, these data demonstrate that the short C-terminal tail of these kinases plays a critical role in determining their cytoplasmic/nuclear localization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Humans
  • Mice
  • Molecular Sequence Data
  • Protein Kinase C / chemistry*
  • Protein Kinase C / metabolism*
  • Protein Kinase D2
  • Protein Kinases / chemistry*
  • Protein Kinases / metabolism*
  • Protein Structure, Tertiary
  • Protein Transport
  • Recombinant Fusion Proteins / metabolism
  • Swiss 3T3 Cells

Substances

  • Protein Kinase D2
  • Recombinant Fusion Proteins
  • Protein Kinases
  • protein kinase C nu
  • Protein Kinase C