Phospholipase C delta 1 requires a pleckstrin homology domain for interaction with the plasma membrane

Biochem J. 1995 Dec 15;312 ( Pt 3)(Pt 3):661-6. doi: 10.1042/bj3120661.

Abstract

The structural requirements of phospholipase C delta 1 for interaction with the plasma membrane were analysed by immunofluorescence after microinjection into living cells. Microinjection of deletion mutants revealed that the region required for membrane attachment and binding of inositol 1,4,5-trisphosphate in vitro corresponded to the pleckstrin homology domain, a structural module described in more than 90 proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Blood Proteins / chemistry*
  • Cell Line
  • Cell Membrane / enzymology*
  • Dogs
  • Gene Deletion
  • Inositol 1,4,5-Trisphosphate / metabolism
  • Isoenzymes / chemistry*
  • Isoenzymes / genetics
  • Isoenzymes / metabolism*
  • Mice
  • Microinjections
  • Molecular Sequence Data
  • Mutagenesis
  • Neuroglia / enzymology
  • PC12 Cells
  • Phosphoproteins*
  • Rats
  • Sequence Homology
  • Structure-Activity Relationship
  • Subcellular Fractions / enzymology
  • Transfection
  • Type C Phospholipases / chemistry*
  • Type C Phospholipases / genetics
  • Type C Phospholipases / metabolism*

Substances

  • Blood Proteins
  • Isoenzymes
  • Phosphoproteins
  • platelet protein P47
  • Inositol 1,4,5-Trisphosphate
  • Type C Phospholipases