A role for phosphatidylinositol transfer protein in secretory vesicle formation

Nature. 1995 Oct 12;377(6549):544-7. doi: 10.1038/377544a0.


Vesicular traffic in eukaryotic cells is characterized by two steps of membrane rearrangement: the formation of vesicles from donor membranes and their fusion with acceptor membranes. With respect to vesicle formation, several of the cytosolic proteins implicated in budding and fission have been identified. A feature common to all these proteins is that their targets, when known, are other proteins rather than lipids. Here we report, using a previously established cell-free system derived from a neuroendocrine cell line, the purification of cytosolic factors that stimulate the formation of constitutive secretory vesicles and immature secretory granules from the trans-Golgi network. One such factor, referred to as CAST1, was identified as the alpha and beta isoforms of the mammalian phosphatidylinositol transfer protein (PtdIns-TP) (refs 3-5). The yeast PtdIns-TP, SEC14p (ref. 6), which has no sequence homology to mammalian PtdIns-TP (refs 7,8), was able to substitute for the mammalian PtdIns-TP in secretory vesicle formation. Our results suggest a highly conserved role for phosphoinositides in vesicle formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cattle
  • Cell-Free System
  • Escherichia coli
  • Golgi Apparatus / physiology*
  • Membrane Proteins*
  • Mice
  • PC12 Cells
  • Phosphatidylinositols / metabolism*
  • Phospholipid Transfer Proteins
  • Rats
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins*


  • Carrier Proteins
  • Membrane Proteins
  • Phosphatidylinositols
  • Phospholipid Transfer Proteins
  • Recombinant Proteins
  • SEC24 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins