A role for phosphatidylinositol transfer protein in secretory vesicle formation. | Academic Article individual record
abstract

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.

author list (cited authors)
Ohashi, M., Jan de Vries, K., Frank, R., Snoek, G., Bankaitis, V., Wirtz, K., & Huttner, W. B.
publication date
1995
publisher
Springer Nature Publisher
published in
NATURE Journal
keywords
  • Rats
  • Animals
  • Golgi Apparatus
  • Cattle
  • PC12 Cells
  • Saccharomyces Cerevisiae Proteins
  • Recombinant Proteins
  • Saccharomyces Cerevisiae
  • Cell-Free System
  • Phospholipid Transfer Proteins
  • Mice
  • Carrier Proteins
  • Phosphatidylinositols
  • Escherichia Coli
  • Membrane Proteins
altmetric score

3.0

citation count

152

PubMed Central ID
7566155
identifier
91820SE
Digital Object Identifier (DOI)
start page
544
end page
547
volume
377
issue
6549