Identification and characterization of nuclear localization signals of CaMKP-N

J Biochem. 2004 Aug;136(2):183-8. doi: 10.1093/jb/mvh109.

Abstract

Calmodulin-dependent protein kinase phosphatase (CaMKP) and CaMKP-N dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases. The enzymatic properties of CaMKP-N and CaMKP resemble each other, whereas their localizations are different. CaMKP-N is localized in the nucleus, whereas CaMKP is localized in the cytosol. In the present study, the nuclear localization signals (NLSs) of CaMKP-N were identified and characterized. CaMKP-N contains two NLSs, NLS1 and NLS2, at the C-terminus. A cluster of basic residues in the NLSs is important for their function. NLS1 and NLS2 function independently, but mutagenesis analysis suggests that these NLSs interact with each other.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cytosol / metabolism
  • Gene Deletion
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Mutation
  • Nuclear Localization Signals
  • Phosphoprotein Phosphatases / chemistry*
  • Phosphoprotein Phosphatases / metabolism
  • Protein Phosphatase 2C
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • Nuclear Localization Signals
  • Green Fluorescent Proteins
  • calmodulin dependent protein kinase II phosphatase
  • Phosphoprotein Phosphatases
  • Protein Phosphatase 2C