Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis.

Published

Journal Article

Inositol polyphosphate 1-phosphatase, an enzyme of the phosphatidylinositol signaling pathway, hydrolyzes the 1-phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. We have used indirect immunofluorescence microscopy, Western blot analysis, and enzyme assays to determine the cellular localization of the enzyme. We find that the enzyme is present, but not exclusively, in the nucleus of Madin-Darby bovine kidney cells, and also in COS-7 and HeLa cells that were transiently transfected with a cDNA encoding bovine inositol polyphosphate 1-phosphatase. DNA synthesis, as measured in COS-7 and HeLa cells transiently over-expressing enzyme, was reduced 50% in cells transfected with wild-type enzyme compared with nontransfected cells or cells transfected with an inactive mutant form of the enzyme. These data demonstrate that this response is mediated by one of the substrates or products of inositol polyphosphate 1-phosphatase. We propose that overexpressed inositol polyphosphate 1-phosphatase degrades a stimulatory inositol phosphate(s) and thereby inhibits DNA synthesis.

Full Text

Duke Authors

Cited Authors

  • York, JD; Saffitz, JE; Majerus, PW

Published Date

  • August 5, 1994

Published In

Volume / Issue

  • 269 / 31

Start / End Page

  • 19992 - 19999

PubMed ID

  • 8051083

Pubmed Central ID

  • 8051083

International Standard Serial Number (ISSN)

  • 0021-9258

Language

  • eng

Conference Location

  • United States