An engineered site for protein kinase C flanking the SV40 large T-antigen NLS confers phorbol ester-inducible nuclear import

Chong Y. Xiao, David A. Jans

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9 Citations (Scopus)

Abstract

Nuclear import of simian virus SV40 large tumour antigen (T-ag) is enhanced by the protein kinase CK2 (CK2) site flanking the nuclear localisation sequence (NLS). We report here that replacement of this site with a consensus site for protein kinase C (PK-C) can alter the regulation of T-ag nuclear import and render it inducible by phorbol ester. Measurement of nuclear import kinetics using fluorescently labelled proteins and confocal laser scanning microscopy show that the introduced PK-C site is functional in enhancing T-ag nuclear import compared to a protein lacking the CK2 site. Treatment with the PK-C activator phorbol 12-myristate 13-acetate (PMA) further increases the level of maximal nuclear accumulation and the initial nuclear import rate. This engineered PMA-responsive NLS may have application in targeting of molecules of interest to the nucleus in response to agents stimulating PK-C. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)313-317
Number of pages5
JournalFEBS Letters
Volume436
Issue number3
DOIs
Publication statusPublished - 9 Oct 1998
Externally publishedYes

Keywords

  • Ca/phospholipid-dependent protein kinase C
  • Confocal laser scanning microscopy
  • Microinjection
  • Nuclear import kinetics
  • Phosphorylation-regulated nuclear localization sequence

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